ID   RECA_CLOPE              Reviewed;         352 AA.
AC   P94666;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=CPE1673;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=9084172; DOI=10.1099/00221287-143-3-885;
RA   Johnston J.L., Sloan J., Fyfe J.A.M., Davies J.K., Rood J.I.;
RT   "The recA gene from Clostridium perfringens is induced by methyl
RT   methanesulphonate and contains an upstream Cheo box.";
RL   Microbiology 143:885-890(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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}.
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DR   EMBL; U61497; AAC45139.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB81379.1; -; Genomic_DNA.
DR   RefSeq; WP_003459804.1; NC_003366.1.
DR   AlphaFoldDB; P94666; -.
DR   SMR; P94666; -.
DR   STRING; 195102.gene:10490937; -.
DR   EnsemblBacteria; BAB81379; BAB81379; BAB81379.
DR   GeneID; 29570973; -.
DR   KEGG; cpe:CPE1673; -.
DR   HOGENOM; CLU_040469_3_2_9; -.
DR   OMA; EGARHMS; -.
DR   Proteomes; UP000000818; 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..352
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122692"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   352 AA;  37955 MW;  B76D0F8B29459666 CRC64;
     MANIDKDKLK AIEMAMGQIE KQFGKGSVMK LGEQGAPQMD AVSTGCLDLD IALGIGGVPK
     GRIIEIYGPE SSGKTTVALH VVAEAQKLGG AAAYIDAEHA LDPVYAKRLG VNIDDLVVSQ
     PDTGEQALEI TEALVRSGAI DVLVVDSVAA LVPRAEIEGE MGDSHVGLQA RLMSQALRKL
     TGTINKSNCV VIFINQLREK VGIMFGNPET TPGGRALKFY ASVRMDIRRI DSIKQGDGIT
     GNRTRVKIVK NKVAPPFKQA EFDIMYNEGI SKEGNIVDVG VKENIVQKSG AWFSYGDIRL
     GQGRENAKQY LKENPAVALD IENQIREKYS LPLAKAVEST SVEENTEESV ES