ID   RECA_RHILV              Reviewed;         351 AA.
AC   P24074;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VF39;
RX   PubMed=1896024; DOI=10.1007/bf00264217;
RA   Selbitschka W., Arnold W., Priefer U.B., Rottschafer T., Schmidt M.,
RA   Simon R., Puehler A.;
RT   "Characterization of recA genes and recA mutants of Rhizobium meliloti and
RT   Rhizobium leguminosarum biovar viciae.";
RL   Mol. Gen. Genet. 229:86-95(1991).
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; X59956; CAA42578.1; -; Genomic_DNA.
DR   PIR; S16896; S16896.
DR   AlphaFoldDB; P24074; -.
DR   SMR; P24074; -.
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..351
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122814"
FT   REGION          330..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   351 AA;  37725 MW;  39FB06D4C7233D53 CRC64;
     MDKSKALEAA LSQIERSFGK GSIMKLGSNE NVVEIETIST GSLGLDIALG VGGLPRGRII
     EIYGPESSGK TTLALQTIAE AQKKGGICAF VDAEHALDPV YARKLGVDLQ NLLISQPDTG
     EQALEITDTL VRSGRVDVLV VDSVAALTPR AEIEGEMGDT VPGLQARLMS QALRKLTASI
     SKSNTMVIFI NQIRMKIGVM FGSPETTTGG NALKFYASVR LDIRRIGAVK EREEVIGNQT
     RVKVVKNKMA PPFKQVEFDI MYGEGVSKTG ELVDLGVKAG IVEKSGAWFS YNSQRLGQGR
     ENAKTFLRDN PDLAREIELS LRQNAGLIAD RFLQNGGPDP DDGDGDATAE M