ID   RECA_CORU7              Reviewed;         371 AA.
AC   B1VDD6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=cu0874;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
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; AM942444; CAQ04834.1; -; Genomic_DNA.
DR   RefSeq; WP_012360123.1; NC_010545.1.
DR   AlphaFoldDB; B1VDD6; -.
DR   SMR; B1VDD6; -.
DR   STRING; 504474.cu0874; -.
DR   EnsemblBacteria; CAQ04834; CAQ04834; cu0874.
DR   GeneID; 60603650; -.
DR   KEGG; cur:cu0874; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_11; -.
DR   OMA; DYGEQAL; -.
DR   OrthoDB; 1080436at2; -.
DR   Proteomes; UP000001727; 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..371
FT                   /note="Protein RecA"
FT                   /id="PRO_1000114327"
FT   REGION          343..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         75..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   371 AA;  39853 MW;  16D9B2B91D3255B2 CRC64;
     MAPKKKATTA AQKDRSKALD LAMAQIEKDF GKGAIMRLGD ENRPPISAIP SGNIAINVAL
     GIGGFPRGRV VEIYGPESSG KTTVALHAIA EAQKGGGIAA FIDAEHALDP EYAKALGVDT
     DALLVSQPDT GEQALEIADM LVRSGAIDMV VIDSVAALTP KAEIDGEMGD SHVGLQARLM
     SQALRKMTSA LYQTGTTAIF INQLREKIGV MFGSPETTTG GKALKFYASV RCDIRRIQAL
     KDGQDVVGNR TRLKIVKNKV SPPFKIAEFD ILYGEGISRE GSILDLGVDA GIIKKSGSWF
     TYEGEQLGQG KEKARDFLKS NPELAEQLDD RIMQELKVGP YAKAKDEPIA DEDQPIDVVP
     NFDDQDVEPQ N