RECA_VIBCH
ID RECA_VIBCH Reviewed; 354 AA.
AC P45383; Q9KUH8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=VC_0543;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=8058040; DOI=10.1007/bf00285457;
RA Stroeher U.H., Lech A.J., Manning P.A.;
RT "Gene sequence of recA+ and construction of recA mutants of Vibrio
RT cholerae.";
RL Mol. Gen. Genet. 244:295-301(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2740-80;
RX PubMed=7828921; DOI=10.1016/0378-1119(94)00686-m;
RA Margraf R.L., Roca A.I., Cox M.M.;
RT "The deduced Vibrio cholerae RecA amino-acid sequence.";
RL Gene 152:135-136(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RA Bhasin N., Gupta N., Ghosh A.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA50764.1; Type=Miscellaneous discrepancy; Note=Submitters have revised their sequence in positions 27, 49, 52 and 64 to agree with the one shown in this entry, but have not submitted the revised DNA sequence.; Evidence={ECO:0000305};
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DR EMBL; X71969; CAA50764.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U10162; AAC43291.1; -; Genomic_DNA.
DR EMBL; L42384; AAB59100.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93711.1; ALT_INIT; Genomic_DNA.
DR PIR; E82310; E82310.
DR PIR; S46274; S46274.
DR AlphaFoldDB; P45383; -.
DR SMR; P45383; -.
DR STRING; 243277.VC_0543; -.
DR DNASU; 2615212; -.
DR EnsemblBacteria; AAF93711; AAF93711; VC_0543.
DR KEGG; vch:VC_0543; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_6; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IMP:TIGR.
DR GO; GO:0006281; P:DNA repair; IMP:TIGR.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..354
FT /note="Protein RecA"
FT /id="PRO_0000122891"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 94
FT /note="A -> T (in Ref. 1; CAA50764)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="C -> Y (in Ref. 4; AAF93711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38250 MW; A1CCEF47C8771A8C CRC64;
MDENKQKALA AALGQIEKQF GKGSIMRLGD NRAMDVETIS TGSLSLDIAL GAGGLPMGRI
VEIFGPESSG KTTLTLELIA AAQREGKTCA FIDAEHALDP VYAKKLGVNI DELLVSQPDT
GEQALEICDA LARSGAVDVI VVDSVAALTP KAEIEGEMGD SHMGLQARML SQAMRKLTGN
LKQSNCMCIF INQIRMKIGV MFGNPETTTG GNALKFYASV RLDIRRTGAI KEGEEVVGNE
TRIKVVKNKI AAPFKEANTQ IMYGQGFNRE GELIDLGVKH KMVEKSGAWY SYNGDKIGQG
KANACKYLKE NPEIAKTLDK KLREMLLNPE NMQLIAETSS AADDVEFGAV PEEF
