ID   RECA_ENTFA              Reviewed;         348 AA.
AC   P42444;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 135.
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=EF_3171;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-192.
RX   PubMed=1556091; DOI=10.1128/jb.174.8.2729-2732.1992;
RA   Dybvig K., Hollingshead S.K., Heath D.G., Clewell D.B., Sun F., Woodard A.;
RT   "Degenerate oligonucleotide primers for enzymatic amplification of recA
RT   sequences from Gram-positive bacteria and mycoplasmas.";
RL   J. Bacteriol. 174:2729-2732(1992).
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. {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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DR   EMBL; AE016830; AAO82845.1; -; Genomic_DNA.
DR   EMBL; M81466; AAA24782.1; -; Genomic_DNA.
DR   PIR; C41846; C41846.
DR   RefSeq; NP_816775.1; NC_004668.1.
DR   RefSeq; WP_002354860.1; NZ_KE136524.1.
DR   AlphaFoldDB; P42444; -.
DR   SMR; P42444; -.
DR   STRING; 226185.EF_3171; -.
DR   EnsemblBacteria; AAO82845; AAO82845; EF_3171.
DR   GeneID; 60892411; -.
DR   KEGG; efa:EF3171; -.
DR   PATRIC; fig|226185.45.peg.406; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_1_2_9; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000001415; Chromosome.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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..348
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122709"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   348 AA;  37410 MW;  E8D4F5ED406842F6 CRC64;
     MADDRKVALD AALKKIEKNF GKGSIMKLGE KADQKISTIP SGSLALDVAL GVGGYPRGRI
     IEVYGPESSG KTTVSLHAIA EVQRNGGTAA FIDAEHALDP QYAEKLGVNI DELLLSQPDT
     GEQGLEIADA LVSSGAIDIV VIDSVAALVP RAEIDGEMGA SHVGLQARLM SQALRKLSGS
     INKTKTIAIF INQIREKVGV MFGNPETTPG GRALKFYATV RLEVRRAEQL KQGTDIVGNR
     TKIKVVKNKV APPFKVAEVD IMYGQGISQE GELLDMAVEK DLISKSGAWY GYKEERIGQG
     RENAKQYMAD HPEMMAEVSK LVRDAYGIGD GSTITEEAEG QEELPLDE