ECOLI:GYRB

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	gyrB (ECO:0000255 with HAMAP-Rule:MF_01898) (synonyms: acrB, himB, hisU, nalC, parA, pcbA)
Protein Name(s)	DNA gyrase subunit B (ECO:0000255 with HAMAP-Rule:MF_01898)
External Links
UniProt	P0AES6
EMBL	X04341 D87842 L10328 U00096 AP009048 M15548
PIR	D65172
RefSeq	YP_026241.1 YP_491736.1
PDB	1AJ6 1EI1 1KZN 3G7E 3NUH 4DUH 4HYP 4KFG 4PRV 4PRX 4PU9
PDBsum	1AJ6 1EI1 1KZN 3G7E 3NUH 4DUH 4HYP 4KFG 4PRV 4PRX 4PU9
ProteinModelPortal	P0AES6
SMR	P0AES6
DIP	DIP-48005N
IntAct	P0AES6
STRING	511145.b3699
BindingDB	P0AES6
ChEMBL	CHEMBL2311224
DrugBank	DB00817
PaxDb	P0AES6
PRIDE	P0AES6
EnsemblBacteria	AAT48201 BAE77595
GeneID	12930543 948211
KEGG	ecj:Y75_p3474 eco:b3699
PATRIC	32122895
EchoBASE	EB0419
EcoGene	EG10424
eggNOG	COG0187
HOGENOM	HOG000075155
InParanoid	P0AES6
KO	K02470
OMA	IFETTEF
OrthoDB	EOG6P334W
PhylomeDB	P0AES6
BioCyc	EcoCyc:EG10424-MONOMER ECOL316407:JW5625-MONOMER MetaCyc:EG10424-MONOMER
EvolutionaryTrace	P0AES6
PRO	PR:P0AES6
Proteomes	UP000000318 UP000000625
Genevestigator	P0AES6
GO	GO:0005694 GO:0005737 GO:0009330 GO:0009295 GO:0005524 GO:0003677 GO:0003918 GO:0008094 GO:0000287 GO:0006200 GO:0007059 GO:0006265 GO:0006268 GO:0046677 GO:0042493 GO:0006351
Gene3D	3.30.230.10 3.30.565.10 3.40.50.670
HAMAP	MF_01898
InterPro	IPR002288 IPR011557 IPR003594 IPR020568 IPR014721 IPR001241 IPR013506 IPR013759 IPR013760 IPR018522 IPR006171
Pfam	PF00204 PF00986 PF02518 PF01751
PRINTS	PR00418
SMART	SM00387 SM00433
SUPFAM	SSF54211 SSF55874 SSF56719
TIGRFAMs	TIGR01059
PROSITE	PS00177 PS50880

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0003916	DNA topoisomerase activity	PMID:24899021^[1]	ECO:0000314			F	The Table and Figure presented in the paper includes the necessary results	complete CACAO 10598
enables	GO:0034335	DNA supercoiling activity	PMID:186775^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	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:EG10424 PANTHER:PTN000018846 UniProtKB:Q9HUJ8	P	Seeded From UniProt	complete
enables	GO:0003918	DNA topoisomerase type II (ATP-hydrolyzing) activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10424 PANTHER:PTN000018846 UniProtKB:O67137 UniProtKB:P9WG45 UniProtKB:Q9HUJ8	F	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:9144789^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0009330	DNA topoisomerase complex (ATP-hydrolyzing)	PMID:347446^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:6094559^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:15535863^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006265	DNA topological change	PMID:6327603^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:7952188^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:9756859^[10]	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:368801^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10764756^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:6294616^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[15]	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:IPR000565 InterPro:IPR001241 InterPro:IPR002288 InterPro:IPR011557 InterPro:IPR013506 InterPro:IPR013759 InterPro:IPR018522	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:IPR000565 InterPro:IPR001241 InterPro:IPR002288 InterPro:IPR011557 InterPro:IPR013506 InterPro:IPR013759 InterPro:IPR013760 InterPro:IPR018522	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:IPR000565 InterPro:IPR001241 InterPro:IPR002288 InterPro:IPR011557 InterPro:IPR013506 InterPro:IPR013759 InterPro:IPR013760 InterPro:IPR018522	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:IPR011557	C	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:IPR000565 InterPro:IPR001241 InterPro:IPR002288 InterPro:IPR011557 InterPro:IPR013506 InterPro:IPR013759 InterPro:IPR018522	P	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:UR000056593	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:UR000056593	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000056593	F	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:UR000056593	P	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:UR000056593	P	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
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
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: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
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:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	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
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Notes

References

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

↑ Galloway-Peña, J et al. (2014) GyrB polymorphisms accurately assign invasive viridans group streptococcal species. J. Clin. Microbiol. 52 2905-12 PubMed GONUTS page
↑ 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
↑ ^3.0 ^3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Tsai, FT et al. (1997) The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin. Proteins 28 41-52 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
↑ 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
↑ 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
↑ Kampranis, SC & Maxwell, A (1998) Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. J. Biol. Chem. 273 26305-9 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
↑ Chatterji, M et al. (2000) The additional 165 amino acids in the B protein of Escherichia coli DNA gyrase have an important role in DNA binding. J. Biol. Chem. 275 22888-94 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
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:24899021-1] Galloway-Peña, J et al. (2014) GyrB polymorphisms accurately assign invasive viridans group streptococcal species. J. Clin. Microbiol. 52 2905-12 PubMed GONUTS page

[PMID:186775-2] 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:21873635-3] 3.0 ^3.1 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:9144789-4] Tsai, FT et al. (1997) The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin. Proteins 28 41-52 PubMed GONUTS page

[PMID:347446-5] 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:6094559-6] 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:15535863-7] Peter, BJ et al. (2004) Genomic transcriptional response to loss of chromosomal supercoiling in Escherichia coli. Genome Biol. 5 R87 PubMed GONUTS page

[PMID:6327603-8] Steck, TR et al. (1984) DNA supercoiling in gyrase mutants. J. Bacteriol. 158 397-403 PubMed GONUTS page

[PMID:7952188-9] 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:9756859-10] Kampranis, SC & Maxwell, A (1998) Hydrolysis of ATP at only one GyrB subunit is sufficient to promote supercoiling by DNA gyrase. J. Biol. Chem. 273 26305-9 PubMed GONUTS page

[PMID:368801-11] 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:10764756-12] Chatterji, M et al. (2000) The additional 165 amino acids in the B protein of Escherichia coli DNA gyrase have an important role in DNA binding. J. Biol. Chem. 275 22888-94 PubMed GONUTS page

[PMID:6294616-13] 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:18304323-14] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-15] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:GYRB

Contents

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