ID   RECA_TROW8              Reviewed;         437 AA.
AC   P65982; Q83MS9; Q83NC6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=TW628;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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; BX251412; CAD67292.1; -; Genomic_DNA.
DR   RefSeq; WP_011096570.1; NC_004551.1.
DR   AlphaFoldDB; P65982; -.
DR   SMR; P65982; -.
DR   GeneID; 67388408; -.
DR   KEGG; tws:TW628; -.
DR   HOGENOM; CLU_040469_3_0_11; -.
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..437
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122888"
FT   REGION          343..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   437 AA;  46450 MW;  969186E5C5F390D8 CRC64;
     MSSNDQINRT RALELALANI DRQYGKGAVM RMNDAQKAYI DVIPTGSIAL DYALGVGGLP
     RGRIVEIYGP ESSGKTTLTL HAIASVQRAG GIAAFIDAEH ALDPEYAKKL GVDIDALLVS
     QPDSGEQALE ISDMLIRSTA IDLIVIDSVA ALVPRAELEG DMGDMHVGLQ ARLMSQALRK
     ITSGLNQTGT TAIFINQLRE KVGVFFGSPE TTPGGRALKF YASVRLDIRR VETIKQGTEA
     VGNRTRVKVV KNKVAPPFKQ AEFDVLYGVG ISRESGLIDF AVDRGIIKKS GSWYVYGDDQ
     LGQGKENARR FLLENKSVAD EIENKIISLL GFRSNEFGDL PDHDAAVRTS PDTNSRKVSG
     TGAVHTTSGS PSAGKGTASG AVNNSRDSTG GDTPAGQGPL NLSVNRDVST DTVSSKISDA
     THNQKPAGNG KSVKRKG