ID   RECA_AQUPY              Reviewed;         348 AA.
AC   P33542;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX   PubMed=7929298; DOI=10.1016/s0021-9258(18)47335-8;
RA   Wetmur J.G., Wong D.M., Ortiz B., Tong J., Reichert F., Gelfand D.H.;
RT   "Cloning, sequencing, and expression of RecA proteins from three distantly
RT   related thermophilic eubacteria.";
RL   J. Biol. Chem. 269:25928-25935(1994).
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; L23135; AAA67702.1; -; Genomic_DNA.
DR   PIR; A55020; A55020.
DR   AlphaFoldDB; P33542; -.
DR   SMR; P33542; -.
DR   PRIDE; P33542; -.
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..348
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122643"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   348 AA;  37913 MW;  31E93930989739ED CRC64;
     MARVSENLSE KMKALEVALS SIEKRFGKGA VMPLKAVETV EVETIPTGSI SLDIATGVGG
     IPKGRITEIF GVESSGKTTL ALHVIAEAQK RGGVAVFIDA EHALDPKYAK KLGVDVDNLY
     ISQPDYGEQA LEIAESLINS GAVDVIVVDS VAALVPKDEL EGEMGEAQVG KQARLMSQAL
     RKLKGAVHRS NTALIFINQI REKIGVMFGN PETTPGGRAL KFFSDMRLEV RRLGDVKEGG
     EKKGYRVKVR VVKNKLAPPF QEAEFDVIYG EGICRICDII DTAANLGVIT KSGSWYSYGE
     KRLGQGREQA KKYLLEHPEM LEEIERKVRE VSGLVRPDTE NSVGEKSE