ID E3DA55_GARV3 Unreviewed; 384 AA. AC E3DA55; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|HAMAP-Rule:MF_00268}; DE AltName: Full=Recombinase A {ECO:0000256|ARBA:ARBA00033319, ECO:0000256|HAMAP-Rule:MF_00268}; GN Name=recA {ECO:0000256|HAMAP-Rule:MF_00268, GN ECO:0000313|EMBL:ADP38949.1}; GN OrderedLocusNames=HMPREF0421_20867 {ECO:0000313|EMBL:ADP38949.1}; OS Gardnerella vaginalis (strain ATCC 14019 / 317). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Gardnerella. OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38949.1, ECO:0000313|Proteomes:UP000001453}; RN [1] {ECO:0000313|EMBL:ADP38949.1, ECO:0000313|Proteomes:UP000001453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453}; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G., RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A., RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E., RA Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial RT differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002104; ADP38949.1; -; Genomic_DNA. DR RefSeq; WP_004113623.1; NC_014644.1. DR RefSeq; YP_003985972.1; NC_014644.1. DR AlphaFoldDB; E3DA55; -. DR GeneID; 60756425; -. DR KEGG; gvg:HMPREF0421_20867; -. DR PATRIC; fig|525284.18.peg.856; -. DR HOGENOM; CLU_040469_3_2_11; -. DR OrthoDB; 9776733at2; -. DR Proteomes; UP000001453; 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}; KW SOS response {ECO:0000256|HAMAP-Rule:MF_00268, KW ECO:0000256|RuleBase:RU000526}. FT DOMAIN 53..212 FT /note="RecA family profile 1" FT /evidence="ECO:0000259|PROSITE:PS50162" FT DOMAIN 217..290 FT /note="RecA family profile 2" FT /evidence="ECO:0000259|PROSITE:PS50163" FT REGION 353..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 83..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268" SQ SEQUENCE 384 AA; 41079 MW; 7A32F4E51E18CA2F CRC64; MAQQAKKGAV DRLIDADKAD PRRKAALETA LANVEKQYGK GSAMRLGDKP LQDVEVIPTG SIALDMALGI GGVPRGRIVE VYGPESSGKT TLALHIVANA QKNGGIAAFI DAEHALDPVY ARKLGVDTDS LIVSQPDNGE QALEIADMLI RSGALDVIVV DSVAALVPKA EIDGDMGDSH VGLQARLMSQ ALRKMTGALS QAGTTAIFIN QLREKIGVFF GNPETTTGGK ALKFYSSVRM DIRRVSTIKN GEEAVGNRTK VKIVKNKMAP PFKTAEFDVL YGEGISTEGS VIDMAVQCDV IKKSGSWFTY EGEQLGQGRE NVRQFLKDNP AITEEISDKV KVAFGLMKPE DQFVEVEDED DNSQSVSSSS ADSKTNTSKG SDVK //