ID   RECA_CAMFE              Reviewed;         345 AA.
AC   O30884;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
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};
OS   Campylobacter fetus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=84-32 / 23D;
RX   PubMed=9393719; DOI=10.1128/jb.179.23.7523-7529.1997;
RA   Dworkin J., Shedd O.L., Blaser M.J.;
RT   "Nested DNA inversion of Campylobacter fetus S-layer genes is recA
RT   dependent.";
RL   J. Bacteriol. 179:7523-7529(1997).
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; AF020677; AAB86923.1; -; Genomic_DNA.
DR   RefSeq; WP_002848230.1; NZ_WLYG01000014.1.
DR   AlphaFoldDB; O30884; -.
DR   SMR; O30884; -.
DR   STRING; 983328.AFGH01000004_gene1014; -.
DR   GeneID; 61064046; -.
DR   OMA; DYGEQAL; -.
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; SOS response.
FT   CHAIN           1..345
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122676"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   345 AA;  37209 MW;  F0AA05048DD4B220 CRC64;
     MDDNKKKSLD LALKQIDKAF GKGTVLRLGD KEIEPIDSIS SGSIGLDIAL GIGGVPKGRI
     VEIYGPESSG KTTLTLHLIA ESQKVGGVCA FVDAEHALDV KYAKNLGVDT DNLYISQPDF
     GEQALDIVET LARSGAVDLI VIDSVAALTP KSEIEGDMGD QHVGLQARLM SQALRKLTGV
     VHKMGTTVVF INQIRMKIGA MGYGTPETTT GGNALKFYAS VRLDVRKIAT LKQSDEPIGN
     RVKVKVVKNK VAPPFRQAEF DIMFGEGISK EGEIIDYGVK LDIIDKSGAW FSYDNSKLGQ
     GRENSKAFLK ENKAIADEIT EKIRANMGDS IMSGAVDEEE MEGDE