ID   RECA_BORHE              Reviewed;         356 AA.
AC   Q8VS69;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Borrelia hermsii.
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15060027; DOI=10.1128/jb.186.8.2266-2274.2004;
RA   Putteet-Driver A.D., Zhong J., Barbour A.G.;
RT   "Transgenic expression of RecA of the spirochetes Borrelia burgdorferi and
RT   Borrelia hermsii in Escherichia coli revealed differences in DNA repair and
RT   recombination phenotypes.";
RL   J. Bacteriol. 186:2266-2274(2004).
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; AF395125; AAL57321.1; -; Genomic_DNA.
DR   RefSeq; WP_012421910.1; NZ_CP014808.1.
DR   AlphaFoldDB; Q8VS69; -.
DR   SMR; Q8VS69; -.
DR   STRING; 140.A0V01_03675; -.
DR   eggNOG; COG0468; Bacteria.
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..356
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122666"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   356 AA;  38750 MW;  E0D2CBCFBC118D2A CRC64;
     MSKLKDNPDN SLNDRLNREK AIELARVQIE KDFGKGSLIK MGESPVGKGI ESISSGSILL
     DEAIGVGGYP RGRIIEIFGP ESSGKTTLTL QAIAEVQKNG GIAAFIDAEH ALDPAYAKAL
     GVNIDELWIS QPDTGEQALE IAEYLIRSGG VDLIVVDSVA ALTPQAEIDG EMGDSQIGLQ
     ARLMSKALRK ITGILSKSNT CIMFINQLRM KIGVMFGNPE TTTGGNALKF YSSLRLEVRK
     IDQVTGSSAD DIVGNKIRIK VVKNKVAPPF RKVELVIYFG KGISREASIL DASVKYNLIQ
     KTGSWYSMGD DKLGQGREHA VSYLVKEKEV TDELESKLRK IIFEDPNQDF LEVGTT