ID   RECA_TREPS              Reviewed;         407 AA.
AC   B2S3T1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=TPASS_0692;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD71110.1; -; Genomic_DNA.
DR   RefSeq; WP_010882137.1; NC_010741.1.
DR   EnsemblBacteria; ACD71110; ACD71110; TPASS_0692.
DR   KEGG; tpp:TPASS_0692; -.
DR   PATRIC; fig|243276.5.peg.733; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000001202; 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..407
FT                   /note="Protein RecA"
FT                   /id="PRO_1000114378"
FT   REGION          358..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   407 AA;  44216 MW;  D9A9861F7B2FF9D1 CRC64;
     MSKALKGDVP VSSSFEEKMK ALEAARLQIE KQFGQGSLMK LGKDDAVQGV EVIPTGNILL
     DEALGIGGYP RGRIIEIFGP ESSGKTTLAL HAVAEAQKRG GIAAFIDAEH ALDPQYAKDL
     GVSVGDLWIS QPDTGEQALE IAESLVRSGA VDIIVVDSVA ALTPQAEIQG DMGDAHVGLI
     ARLMSQALRK LTSIINKSKC TLIFINQLRM KIGIMFGNPE TTTGGIALKF YSSVRIEVRK
     VETLSRGDEE AWGNKVRIRI VKNKMAPPFR KVETEILFGK GFSAFSCLLD AAVKQEIIEK
     KGAWYAYREE KIGQGRDNAV GFLQQNMDIT LEIERAVRTK LFPKQAFISS FQEHRPALSL
     EASPEESDAK TLRRXASRGA GASSSRVQEG SAANDHFQDE STTAKLL