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Database: UniProt
Entry: A0A1G6S1H5_9BURK
LinkDB: A0A1G6S1H5_9BURK
Original site: A0A1G6S1H5_9BURK 
ID   A0A1G6S1H5_9BURK        Unreviewed;       371 AA.
AC   A0A1G6S1H5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=SAMN05192589_104312 {ECO:0000313|EMBL:SDD10772.1};
OS   Paracidovorax valerianellae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=187868 {ECO:0000313|EMBL:SDD10772.1, ECO:0000313|Proteomes:UP000198781};
RN   [1] {ECO:0000313|EMBL:SDD10772.1, ECO:0000313|Proteomes:UP000198781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16619 {ECO:0000313|EMBL:SDD10772.1,
RC   ECO:0000313|Proteomes:UP000198781};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025580,
CC       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; FMZC01000004; SDD10772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6S1H5; -.
DR   STRING; 187868.SAMN05192589_104312; -.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000198781; 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|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
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:UP000198781};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          49..208
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          213..286
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   371 AA;  39597 MW;  1C4BCB59C3036B1C CRC64;
     MDFAVKGTHP AQPVNTEKAK ALQAALAQIE KQFGKGTIMR LGEGEVIEDI QVVSTGSLGL
     DIALGVGGLP RGRVVEIYGP ESSGKTTLTL QVIAEMQKQG GQCAFVDAEH ALDVQYAQKL
     GVQLSDLLIS QPDTGEQALE IVDSLVRSGA VDLIVIDSVA ALTPKAEIEG EMGDSLPGLQ
     ARLMSQALRK LTATIKKTNC MVIFINQIRM KIGVMFGSPE TTTGGNALKF YASVRLDIRR
     TGTIKKGDEA IGNETKVKVV KNKVSPPFKT AEFDILFGEG ISREGEIIDM GVNAKIVEKS
     GAWYAYNGEK IGQGRDNARE FLRENADLAR EIENKVRDSL GIALLPAAIE APAATSGKET
     GKDTAKDAAE K
//
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