ID   RECA_CAMJJ              Reviewed;         343 AA.
AC   A1W1S5; P42440; Q9PM04;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
GN   OrderedLocusNames=CJJ81176_1669;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8300203; DOI=10.1128/iai.62.2.426-432.1994;
RA   Guerry P., Pope P.M., Burr D.H., Leifer J., Joseph S.W., Bourgeois A.L.;
RT   "Development and characterization of recA mutants of Campylobacter jejuni
RT   for inclusion in attenuated vaccines.";
RL   Infect. Immun. 62:426-432(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; U03121; AAA17793.1; -; Unassigned_DNA.
DR   EMBL; CP000538; EAQ72720.1; -; Genomic_DNA.
DR   PIR; I40770; I40770.
DR   RefSeq; WP_002851424.1; NC_008787.1.
DR   AlphaFoldDB; A1W1S5; -.
DR   SMR; A1W1S5; -.
DR   STRING; 354242.CJJ81176_1669; -.
DR   EnsemblBacteria; EAQ72720; EAQ72720; CJJ81176_1669.
DR   KEGG; cjj:CJJ81176_1669; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_1_2_7; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000000646; 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; SOS response.
FT   CHAIN           1..343
FT                   /note="Protein RecA"
FT                   /id="PRO_0000285824"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   CONFLICT        217
FT                   /note="F -> I (in Ref. 1; AAA17793)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  37049 MW;  B5E7FE7FAF424598 CRC64;
     MDDNKRKSLD AALKSLDKTF GKGTILRLGD KEVEQIDSIG TGSVGLDLAL GIGGVPKGRI
     IEIYGPESSG KTTLTLHIIA ECQKAGGVCA FIDAEHALDV KYAKNLGVNT DDLYVSQPDF
     GEQALEIVET IARSGAVDLI VVDSVAALTP KAEIEGDMGD QHVGLQARLM SQALRKLTGI
     VHKMNTTVIF INQIRMKIGA MGYGTPETTT GGNALKFYAS VRLDVRKVAT LKQNEEPIGN
     RVKVKVVKNK VAPPFRQAEF DVMFGEGLSR EGELIDYGVK LDIVDKSGAW FSYKDKKLGQ
     GRENSKAFLK ENPEIADEIT KAIQNSMGIE GMISGSEDDE GEE