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 12-OCT-2022, entry version 122. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 69459402; -. 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 //