ID   RECA_RHIET              Reviewed;         361 AA.
AC   P24543;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 108.
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 etli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=29449;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNPAF512;
RX   PubMed=1832737; DOI=10.1007/bf00260644;
RA   Michiels J., Vande Broek A., Vanderleyden J.;
RT   "Molecular cloning and nucleotide sequence of the Rhizobium phaseoli recA
RT   gene.";
RL   Mol. Gen. Genet. 228:486-490(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Michiels J.;
RL   Submitted (FEB-1995) 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. {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}.
CC   -!- CAUTION: Strain CNPAF512 was originally thought to originate from
CC       R.leguminosarum bv phaseoli. {ECO:0000305}.
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DR   EMBL; X62479; CAA44346.1; -; Genomic_DNA.
DR   PIR; S17782; S17782.
DR   AlphaFoldDB; P24543; -.
DR   SMR; P24543; -.
DR   STRING; 491916.RHECIAT_CH0002420; -.
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..361
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122812"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   361 AA;  38673 MW;  CCC86C6F3735B880 CRC64;
     MSQNSLRLVE DKSVDKSKAL EAALSQIERS FGKGSIMKLG SNENVIEIET ISTGSLGLDI
     ALGVGGLPKG RIIEIYGPES SGKTTLALQT IAESQKKGGI CAFVDAEHAL DPVYARKLGV
     DLQNLLISQP DTGEQALEIT DTLVRSGAVD VLVVDSVAAL TPRAEIEGEM GDSLPGLQAR
     LMSQALRKLT ASISKSNTMV IFINQIRMKI GVMFGSPETT TGGNALKFYA SVRLDIRRIG
     SVKEREEVIG NQTRVKVVKN KMAPPFKQVE FDIMYGEGVS KTGELVDLGV KAGIVEKSGA
     WFSYNSQRLG QGGENAKTFL RDNPDLAREI ELALRENAGL IADRFLQNGG PDADDGDGAD
     M