ECOLI:GYRA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	gyrA (ECO:0000255 with HAMAP-Rule:MF_01897) (synonyms: hisW, nalA, parD)
Protein Name(s)	DNA gyrase subunit A (ECO:0000255 with HAMAP-Rule:MF_01897)
External Links
UniProt	P0AES4
EMBL	X06373 X06744 M15631 U00096 AP009048 Y00544
PIR	S02340
RefSeq	NP_416734.1 YP_490470.1
PDB	1AB4 1X75 1ZI0 2Y3P 3NUH 4ELY
PDBsum	1AB4 1X75 1ZI0 2Y3P 3NUH 4ELY
ProteinModelPortal	P0AES4
SMR	P0AES4
DIP	DIP-36179N
IntAct	P0AES4
MINT	MINT-201682
STRING	511145.b2231
BindingDB	P0AES4
ChEMBL	CHEMBL2311224
SWISS-2DPAGE	P0AES4
PaxDb	P0AES4
PRIDE	P0AES4
EnsemblBacteria	AAC75291 BAA16048
GeneID	12933138 946614
KEGG	ecj:Y75_p2193 eco:b2231
PATRIC	32119821
EchoBASE	EB0418
EcoGene	EG10423
eggNOG	COG0188
HOGENOM	HOG000076278
InParanoid	P0AES4
KO	K02469
OMA	KVYWLKV
OrthoDB	EOG661H5V
PhylomeDB	P0AES4
BioCyc	EcoCyc:EG10423-MONOMER ECOL316407:JW2225-MONOMER MetaCyc:EG10423-MONOMER
EvolutionaryTrace	P0AES4
PRO	PR:P0AES4
Proteomes	UP000000318 UP000000625
Genevestigator	P0AES4
GO	GO:0005694 GO:0005737 GO:0009330 GO:0016020 GO:0009295 GO:0005524 GO:0003677 GO:0003918 GO:0008094 GO:0042802 GO:0006200 GO:0007059 GO:0006265 GO:0006268 GO:0046677 GO:0042493 GO:0006351
Gene3D	1.10.268.10 3.30.1360.40 3.90.199.10
HAMAP	MF_01897
InterPro	IPR024946 IPR005743 IPR006691 IPR002205 IPR013758 IPR013757 IPR013760
Pfam	PF03989 PF00521
SMART	SM00434
SUPFAM	SSF56719
TIGRFAMs	TIGR01063

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0034335	DNA supercoiling activity	PMID:186775^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	PMID:186775^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0009330	DNA topoisomerase complex (ATP-hydrolyzing)	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10686 PANTHER:PTN001607041 UniProtKB:O67108	C	Seeded From UniProt	complete
involved_in	GO:0006265	DNA topological change	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10423 EcoGene:EG10686 PANTHER:PTN001607041 UniProtKB:P9WG47 UniProtKB:Q8I0X3 UniProtKB:Q9HUK1	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10423 EcoGene:EG10686 PANTHER:PTN000018855	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001607041 UniProtKB:P9WG47 UniProtKB:Q8I0X3	F	Seeded From UniProt	complete
contributes_to	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10423 EcoGene:EG10686 PANTHER:PTN001607041 UniProtKB:O67108 UniProtKB:P9WG47 UniProtKB:Q9HUK1	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10423 EcoGene:EG10686 PANTHER:PTN001607041	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19834901^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AES4	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AES4	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15698572^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AES4	F	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:770163^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:6178722^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:4208771^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:6094559^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:15535863^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:347446^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006265	DNA topological change	PMID:6327603^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:7952188^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	PMID:368801^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:6294616^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:1851291^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002205 InterPro:IPR005743 InterPro:IPR006691 InterPro:IPR013757 InterPro:IPR013758	F	Seeded From UniProt	complete
enables	GO:0003916	DNA topoisomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006691	F	Seeded From UniProt	complete
enables	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002205 InterPro:IPR005743 InterPro:IPR013757 InterPro:IPR013758 InterPro:IPR013760	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002205 InterPro:IPR005743 InterPro:IPR006691 InterPro:IPR013757 InterPro:IPR013758 InterPro:IPR013760	F	Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005743 InterPro:IPR006691	C	Seeded From UniProt	complete
involved_in	GO:0006259	DNA metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013758	P	Seeded From UniProt	complete
involved_in	GO:0006265	DNA topological change	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002205 InterPro:IPR005743 InterPro:IPR006691 InterPro:IPR013758	P	Seeded From UniProt	complete
involved_in	GO:0006265	DNA topological change	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	F	Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	F	Seeded From UniProt	complete
enables	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000087086	C	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0003916	DNA topoisomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0799	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
involved_in	GO:0046677	response to antibiotic	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0046	P	Seeded From UniProt	complete
	GO:0003918	DNA topoisomerase (ATP-hydrolyzing) activity	PMID:186775^[1]	ECO:0000314			F	figure 3d shows that a high amount of gryase contained only negative supercoiled DNA.	complete CACAO 4536
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Gellert, M et al. (1976) DNA gyrase: an enzyme that introduces superhelical turns into DNA. Proc. Natl. Acad. Sci. U.S.A. 73 3872-6 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rajagopala, SV et al. (2009) Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins. Proteomics 9 5296-302 PubMed GONUTS page
↑ Costenaro, L et al. (2005) Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit. Structure 13 287-96 PubMed GONUTS page
↑ Staudenbauer, WL (1976) Replication of Escherichia coli DNA in vitro: inhibition by oxolinic acid. Eur. J. Biochem. 62 491-7 PubMed GONUTS page
↑ Chao, L & Tillman, DM (1982) Enhanced resistance to nitrosoguanidine killing and mutagenesis in a DNA gyrase mutant of Escherichia coli. J. Bacteriol. 151 764-70 PubMed GONUTS page
↑ Bourguignon, GJ et al. (1973) Studies on the mechanism of action of nalidixic acid. Antimicrob. Agents Chemother. 4 479-86 PubMed GONUTS page
↑ Maxwell, A & Gellert, M (1984) The DNA dependence of the ATPase activity of DNA gyrase. J. Biol. Chem. 259 14472-80 PubMed GONUTS page
↑ Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed GONUTS page
↑ Higgins, NP et al. (1978) Purification of subunits of Escherichia coli DNA gyrase and reconstitution of enzymatic activity. Proc. Natl. Acad. Sci. U.S.A. 75 1773-7 PubMed GONUTS page
↑ Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed GONUTS page
↑ Thornton, M et al. (1994) Immunogold localization of GyrA and GyrB proteins in Escherichia coli. Microbiology (Reading, Engl.) 140 ( Pt 9) 2371-82 PubMed GONUTS page
↑ Sugino, A et al. (1978) Energy coupling in DNA gyrase and the mechanism of action of novobiocin. Proc. Natl. Acad. Sci. U.S.A. 75 4838-42 PubMed GONUTS page
↑ Higgins, NP & Cozzarelli, NR (1982) The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Nucleic Acids Res. 10 6833-47 PubMed GONUTS page
↑ Reece, RJ & Maxwell, A (1991) The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Nucleic Acids Res. 19 1399-405 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:186775-1] 1.0 ^1.1 ^1.2 Gellert, M et al. (1976) DNA gyrase: an enzyme that introduces superhelical turns into DNA. Proc. Natl. Acad. Sci. U.S.A. 73 3872-6 PubMed GONUTS page

[PMID:16858726-2] 2.0 ^2.1 ^2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:19834901-4] Rajagopala, SV et al. (2009) Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins. Proteomics 9 5296-302 PubMed GONUTS page

[PMID:15698572-5] Costenaro, L et al. (2005) Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit. Structure 13 287-96 PubMed GONUTS page

[PMID:770163-6] Staudenbauer, WL (1976) Replication of Escherichia coli DNA in vitro: inhibition by oxolinic acid. Eur. J. Biochem. 62 491-7 PubMed GONUTS page

[PMID:6178722-7] Chao, L & Tillman, DM (1982) Enhanced resistance to nitrosoguanidine killing and mutagenesis in a DNA gyrase mutant of Escherichia coli. J. Bacteriol. 151 764-70 PubMed GONUTS page

[PMID:4208771-8] Bourguignon, GJ et al. (1973) Studies on the mechanism of action of nalidixic acid. Antimicrob. Agents Chemother. 4 479-86 PubMed GONUTS page

[PMID:6094559-9] Maxwell, A & Gellert, M (1984) The DNA dependence of the ATPase activity of DNA gyrase. J. Biol. Chem. 259 14472-80 PubMed GONUTS page

[PMID:15535863-10] Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed GONUTS page

[PMID:347446-11] Higgins, NP et al. (1978) Purification of subunits of Escherichia coli DNA gyrase and reconstitution of enzymatic activity. Proc. Natl. Acad. Sci. U.S.A. 75 1773-7 PubMed GONUTS page

[PMID:6327603-12] Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed GONUTS page

[PMID:7952188-13] Thornton, M et al. (1994) Immunogold localization of GyrA and GyrB proteins in Escherichia coli. Microbiology (Reading, Engl.) 140 ( Pt 9) 2371-82 PubMed GONUTS page

[PMID:368801-14] Sugino, A et al. (1978) Energy coupling in DNA gyrase and the mechanism of action of novobiocin. Proc. Natl. Acad. Sci. U.S.A. 75 4838-42 PubMed GONUTS page

[PMID:6294616-15] Higgins, NP & Cozzarelli, NR (1982) The binding of gyrase to DNA: analysis by retention by nitrocellulose filters. Nucleic Acids Res. 10 6833-47 PubMed GONUTS page

[PMID:1851291-16] Reece, RJ & Maxwell, A (1991) The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Nucleic Acids Res. 19 1399-405 PubMed GONUTS page

[PMID:18304323-17] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

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ECOLI:GYRA

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