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Database: UniProt
Entry: A0A143BKL6_9BACT
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ID   A0A143BKL6_9BACT        Unreviewed;       347 AA.
AC   A0A143BKL6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=GEMMAAP_09965 {ECO:0000313|EMBL:AMW05062.1};
OS   Gemmatimonas phototrophica.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05062.1, ECO:0000313|Proteomes:UP000076404};
RN   [1] {ECO:0000313|EMBL:AMW05062.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05062.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA   Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT   "Functional type 2 photosynthetic reaction centers found in the rare
RT   bacterial phylum Gemmatimonadetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN   [2] {ECO:0000313|EMBL:AMW05062.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05062.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA   Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT   "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT   bacteria in diverse environments.";
RL   Environ. Microbiol. Rep. 8:139-149(2016).
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}.
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DR   EMBL; CP011454; AMW05062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143BKL6; -.
DR   STRING; 1379270.GEMMAAP_09965; -.
DR   KEGG; gph:GEMMAAP_09965; -.
DR   eggNOG; COG0468; Bacteria.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000076404; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          40..199
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          204..277
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   347 AA;  36944 MW;  9B7FB29E3A14765F CRC64;
     MAGSVITDDK RKALALAVAQ IEKSCGKGSI MRLGTDSKVR VESIPTGAIN LDAAIGVGGI
     PRGRITEIYG PESSGKTTLC LHVVANAQRA GGVAAYIDAE HALDTEYAKK LGVDIENLLI
     SQPDTGEQAL EICEILVRSG AVDVIVIDSV AALVPKAEIE GDMGDSHVGL QARLMSQALR
     KLTGAIARSK VSVVFINQLR EKIGVMFGNP ETTTGGKALK FYASLRLDIR RIGPVKEKED
     VIGSHVRVKV VKNKVAPPFK QAEFDIMYAE GISHTSLLVD IGAESGIIDK AGAWYSYGSQ
     RIGQGRENAK MFLKDNPVLM AEIEEKVKVV LGMTAPAPNA PADEVEE
//
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