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Database: UniProt
Entry: A0A0G1KC53_9BACT
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ID   A0A0G1KC53_9BACT        Unreviewed;       336 AA.
AC   A0A0G1KC53;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268};
GN   ORFNames=UW79_C0026G0003 {ECO:0000313|EMBL:KKT81125.1};
OS   Candidatus Yanofskybacteria bacterium GW2011_GWA2_44_9.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1619025 {ECO:0000313|EMBL:KKT81125.1, ECO:0000313|Proteomes:UP000034032};
RN   [1] {ECO:0000313|EMBL:KKT81125.1, ECO:0000313|Proteomes:UP000034032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|ARBA:ARBA00009391,
CC       ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU004527}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKT81125.1}.
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DR   EMBL; LCJR01000026; KKT81125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1KC53; -.
DR   PATRIC; fig|1619025.3.peg.889; -.
DR   Proteomes; UP000034032; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR049261; RecA-like_C.
DR   InterPro; IPR049428; RecA-like_N.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C_sf.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR02012; tigrfam_recA; 1.
DR   PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45900; RECA; 1.
DR   Pfam; PF00154; RecA; 1.
DR   Pfam; PF21096; RecA_C; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54752; RecA protein, C-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00268}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          41..200
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          205..278
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   336 AA;  36448 MW;  B5A040357C54F436 CRC64;
     MSKKSEAQTV KNKNVDLTIK EIQEKYGDGS IMKLGEVGRV DVDVIPTGSL SLDLALGVGG
     VPRGRIIEVY GPESSGKTTL CLHIVSEAQK TGGVAAYVDA EHALDPEYAK KIGVKIDQLL
     ISQPDTGEQA LDIVEALVKS GGVDVVIVDS VAALTPRAEI EGEMDQQHMG LQARLMSHAL
     RKLTAIVAKS KTTVIFINQL RMKIGIMFGN PETTPGGMAL KFYSSVRIEV RKAAQIQAGE
     KIVGNRVKVK IVKNKVAPPF RTCEFDILYN EGISRYADVI NAGVHYNVVT KSGSWFNYGD
     QKLGQGIEGS RQFLKENPKL EKEIVSKIKE VAAKEA
//
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