ECOLI:RECA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	recA (ECO:0000255 with HAMAP-Rule:MF_00268) (synonyms: lexB, recH, rnmB, tif, umuB, zab)
Protein Name(s)	Protein RecA (ECO:0000255 with HAMAP-Rule:MF_00268) Recombinase A (ECO:0000255 with HAMAP-Rule:MF_00268)
External Links
UniProt	P0A7G6
EMBL	V00328 U00096 AP009048
PIR	G65049
RefSeq	NP_417179.1 YP_490908.1
PDB	1AA3 1N03 1REA 1U94 1U98 1U99 1XMS 1XMV 2REB 2REC 3CMT 3CMU 3CMV 3CMW 3CMX
PDBsum	1AA3 1N03 1REA 1U94 1U98 1U99 1XMS 1XMV 2REB 2REC 3CMT 3CMU 3CMV 3CMW 3CMX
ProteinModelPortal	P0A7G6
SMR	P0A7G6
DIP	DIP-31832N
IntAct	P0A7G6
MINT	MINT-1300726
STRING	511145.b2699
BindingDB	P0A7G6
ChEMBL	CHEMBL3434
SWISS-2DPAGE	P0A7G6
PaxDb	P0A7G6
PRIDE	P0A7G6
EnsemblBacteria	AAC75741 BAA16561
GeneID	12930224 947170
KEGG	ecj:Y75_p2637 eco:b2699
PATRIC	32120796
EchoBASE	EB0816
EcoGene	EG10823
eggNOG	COG0468
HOGENOM	HOG000264120
InParanoid	P0A7G6
KO	K03553
OMA	YGEGINT
OrthoDB	EOG6ZKXNZ
PhylomeDB	P0A7G6
BioCyc	EcoCyc:EG10823-MONOMER ECOL316407:JW2669-MONOMER
EvolutionaryTrace	P0A7G6
PRO	PR:P0A7G6
Proteomes	UP000000318 UP000000625
Genevestigator	P0A7G6
GO	GO:0005737 GO:0005524 GO:0003684 GO:0008094 GO:0003697 GO:0048870 GO:0006974 GO:0006310 GO:0006281 GO:0010212 GO:0009432
Gene3D	3.30.250.10 3.40.50.300
HAMAP	MF_00268
InterPro	IPR003593 IPR013765 IPR020584 IPR027417 IPR020588 IPR023400 IPR020587
PANTHER	PTHR22942:SF1
Pfam	PF00154
PRINTS	PR00142
SMART	SM00382
SUPFAM	SSF52540 SSF54752
TIGRFAMs	TIGR02012
PROSITE	PS00321 PS50162 PS50163

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0009432	SOS response	PMID:21764927^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	PMID:21912525^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000534715 UniProtKB:P9WHJ3	C	Seeded From UniProt	complete
involved_in	GO:0048870	cell motility	PMID:17391508^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	PMID:4600265^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:11967071^[6]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:10760155^[7]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:19820696^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0010212	response to ionizing radiation	PMID:24596148^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020584 InterPro:IPR020587 InterPro:IPR020588	F	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013765	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:IPR013765 InterPro:IPR020584 InterPro:IPR020587 InterPro:IPR020588	F	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:IPR020584 InterPro:IPR020587	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013765 InterPro:IPR020588	P	Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020584 InterPro:IPR020587 InterPro:IPR020588	F	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	P	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	P	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	F	Seeded From UniProt	complete
	GO:0006310	DNA recombination	PMID:21912525^[2]	ECO:0000315			P	Figure 5B showed all three mutant strains had reduced recombination efficiency of RecA	complete CACAO 3951
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	C	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	P	Seeded From UniProt	complete
	GO:0009432	SOS response	PMID:21764927^[1]	ECO:0000315			P	Fig. 4: Shows effects of mutations in RecA loading functions on cSOS expression in recA730 mutants	complete CACAO 4431
enables	GO:0008094	DNA-dependent ATPase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	F	Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000083075	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:UR000083075	F	Seeded From UniProt	complete
	GO:0017111	nucleoside-triphosphatase activity	PMID:7021552^[11]	ECO:0000314			F	Table 2 (II) shows that nucleoside triphosphates were catalyzed by protein RecA	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
	GO:0009432	SOS response	PMID:19419960^[12]	ECO:0000315			P	FIGURE 1 shows fluorescent proteins fused to RecA partially suppress the UV sensitivity and SOS induction defects of a recA− strain.	complete
	GO:0008094	DNA-dependent ATPase activity	PMID:19419960^[12]	ECO:0000314			F	FIGURE 3 shows purified RecA-RFP protein possesses ssDNA-dependent ATP and dATP hydrolysis activities.	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
involved_in	GO:0006310	DNA recombination	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0233	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	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
	GO:0003677	DNA repair	PMID:24036048^[13]	ECO:0000314			P	Fig. 5 Shows RecA activity with regards to different temperature at constant pH. Measured by CD spectra	complete CACAO 8648
involved_in	GO:0009432	SOS response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0742	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
	GO:0006310	DNA recombination	PMID:1400177^[14]	ECO:0000315			P	Table 2 shows that mutant recA phenotypes altered the effectiveness of recombination.	complete
	GO:0008094	DNA-dependent ATPase activity	PMID:2951381^[15]	ECO:0000314			F	Figure 1 and Figure 2	complete
	GO:0009432	SOS response	PMID:1400177^[14]	ECO:0000315			P	Figure 1 shows that mutant phenotypes of recA do not induce a SOS response as strong as wild type recA.	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 Vlašić, I et al. (2011) Genetic requirements for high constitutive SOS expression in recA730 mutants of Escherichia coli. J. Bacteriol. 193 4643-51 PubMed GONUTS page
↑ ^2.0 ^2.1 Adikesavan, AK et al. (2011) Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites. PLoS Genet. 7 e1002244 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Gómez-Gómez, JM et al. (2007) A novel role for RecA under non-stress: promotion of swarming motility in Escherichia coli K-12. BMC Biol. 5 14 PubMed GONUTS page
↑ Witkin, EM (1974) Thermal enhancement of ultraviolet mutability in a tif-1 uvrA derivative of Escherichia coli B-r: evidence that ultraviolet mutagenesis depends upon an inducible function. Proc. Natl. Acad. Sci. U.S.A. 71 1930-4 PubMed GONUTS page
↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
↑ Fernández De Henestrosa, AR et al. (2000) Identification of additional genes belonging to the LexA regulon in Escherichia coli. Mol. Microbiol. 35 1560-72 PubMed GONUTS page
↑ Roy, R et al. (2009) SSB protein diffusion on single-stranded DNA stimulates RecA filament formation. Nature 461 1092-7 PubMed GONUTS page
↑ Byrne, RT et al. (2014) Evolution of extreme resistance to ionizing radiation via genetic adaptation of DNA repair. Elife 3 e01322 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Weinstock, GM et al. (1981) Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis. J. Biol. Chem. 256 8829-34 PubMed GONUTS page
↑ ^12.0 ^12.1 Handa, N et al. (2009) Single molecule analysis of a red fluorescent RecA protein reveals a defect in nucleoprotein filament nucleation that relates to its reduced biological functions. J. Biol. Chem. 284 18664-73 PubMed GONUTS page
↑ Metrick, MA et al. (2013) The effects of buffers and pH on the thermal stability, unfolding and substrate binding of RecA. Biophys. Chem. 184 29-36 PubMed GONUTS page
↑ ^14.0 ^14.1 Larminat, F et al. (1992) New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity. J. Bacteriol. 174 6264-9 PubMed GONUTS page
↑ Brenner, SL et al. (1987) recA protein-promoted ATP hydrolysis occurs throughout recA nucleoprotein filaments. J. Biol. Chem. 262 4011-6 PubMed GONUTS page

[PMID:21764927-1] 1.0 ^1.1 Vlašić, I et al. (2011) Genetic requirements for high constitutive SOS expression in recA730 mutants of Escherichia coli. J. Bacteriol. 193 4643-51 PubMed GONUTS page

[PMID:21912525-2] 2.0 ^2.1 Adikesavan, AK et al. (2011) Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites. PLoS Genet. 7 e1002244 PubMed GONUTS page

[PMID:21873635-3] 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:17391508-4] Gómez-Gómez, JM et al. (2007) A novel role for RecA under non-stress: promotion of swarming motility in Escherichia coli K-12. BMC Biol. 5 14 PubMed GONUTS page

[PMID:4600265-5] Witkin, EM (1974) Thermal enhancement of ultraviolet mutability in a tif-1 uvrA derivative of Escherichia coli B-r: evidence that ultraviolet mutagenesis depends upon an inducible function. Proc. Natl. Acad. Sci. U.S.A. 71 1930-4 PubMed GONUTS page

[PMID:11967071-6] Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page

[PMID:10760155-7] Fernández De Henestrosa, AR et al. (2000) Identification of additional genes belonging to the LexA regulon in Escherichia coli. Mol. Microbiol. 35 1560-72 PubMed GONUTS page

[PMID:19820696-8] Roy, R et al. (2009) SSB protein diffusion on single-stranded DNA stimulates RecA filament formation. Nature 461 1092-7 PubMed GONUTS page

[PMID:24596148-9] Byrne, RT et al. (2014) Evolution of extreme resistance to ionizing radiation via genetic adaptation of DNA repair. Elife 3 e01322 PubMed GONUTS page

[PMID:27718375-10] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:7021552-11] Weinstock, GM et al. (1981) Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Characterization of ATP hydrolysis. J. Biol. Chem. 256 8829-34 PubMed GONUTS page

[PMID:19419960-12] 12.0 ^12.1 Handa, N et al. (2009) Single molecule analysis of a red fluorescent RecA protein reveals a defect in nucleoprotein filament nucleation that relates to its reduced biological functions. J. Biol. Chem. 284 18664-73 PubMed GONUTS page

[PMID:24036048-13] Metrick, MA et al. (2013) The effects of buffers and pH on the thermal stability, unfolding and substrate binding of RecA. Biophys. Chem. 184 29-36 PubMed GONUTS page

[PMID:1400177-14] 14.0 ^14.1 Larminat, F et al. (1992) New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity. J. Bacteriol. 174 6264-9 PubMed GONUTS page

[PMID:2951381-15] Brenner, SL et al. (1987) recA protein-promoted ATP hydrolysis occurs throughout recA nucleoprotein filaments. J. Biol. Chem. 262 4011-6 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

ECOLI:RECA

Contents

Annotations

Notes

References

a

b

c

d

e

g

n

p

r

s

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools