ID   RECA_CORP2              Reviewed;         369 AA.
AC   P48288; D9QAZ4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=CpC231_1246;
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=681645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C231;
RX   PubMed=8810496; DOI=10.1111/j.1574-6968.1996.tb08421.x;
RA   Pogson C.A., Simmons C.P., Strugnell R.A., Hodgson A.L.M.;
RT   "Cloning and manipulation of the Corynebacterium pseudotuberculosis recA
RT   gene for live vaccine vector development.";
RL   FEMS Microbiol. Lett. 142:139-145(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231;
RX   PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA   Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA   Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA   Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA   Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA   Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA   Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA   Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA   Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA   Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA   Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA   Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT   "Evidence for reductive genome evolution and lateral acquisition of
RT   virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
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; U30387; AAA82608.1; -; Genomic_DNA.
DR   EMBL; CP001829; ADL10720.1; -; Genomic_DNA.
DR   RefSeq; WP_013242109.1; NC_017301.2.
DR   AlphaFoldDB; P48288; -.
DR   SMR; P48288; -.
DR   STRING; 1719.CPTC_01823; -.
DR   EnsemblBacteria; ADL10720; ADL10720; CpC231_1246.
DR   GeneID; 12298394; -.
DR   KEGG; cpq:CPC231_06325; -.
DR   PATRIC; fig|681645.3.peg.1305; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_11; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000000276; 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..369
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122698"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   369 AA;  39620 MW;  47289A6F58CD02BC CRC64;
     MAAKKNSKSQ PATGDNRQKA LDAALAMIEK DFGKGAVMRL GDDNRPPISA ISSGNTAIDV
     ALGIGGFPKG RIVEVYGPES SGKTTVALHA IAQAQRAGGI AAFIDAEHAL DPDYARKLGV
     DTDALLVSQP DTGEQALEIA DMLVRSGAID IIVIDSVAAL TPKAEIEGEM GDSHVGLQAR
     LMSQALRKMT GALYNSGTTA IFINQLREKI GVMFGSPETT TGGKALKFYA SVRCDVRRIQ
     TLKDGQDAIG NRTRLKVVKN KVSPPFKIAE FDIMYGEGIS RESSIIDLGV DNGIIKKSGS
     WFTYDGDQLG QGKEKVRLYL KQTPELADEI EEKIFRALQI GKYANQNDAL TDDPVDMVPN
     IDFDDEDNG