ID D1J6P5_9PROT Unreviewed; 432 AA. AC D1J6P5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 11-DEC-2019, entry version 36. DE RecName: Full=UvrABC system protein A {ECO:0000256|SAAS:SAAS00088996}; OS Acetobacter estunensis. OG Plasmid pGP2 {ECO:0000313|EMBL:CBI12145.1}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=104097 {ECO:0000313|EMBL:CBI12145.1}; RN [1] {ECO:0000313|EMBL:CBI12145.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GP2 {ECO:0000313|EMBL:CBI12145.1}; RC PLASMID=pGP2 {ECO:0000313|EMBL:CBI12145.1}; RA Grones P., Grones J.; RT "Nucleotide sequence analysis of small cryptic plasmid pGP2 from RT Acetobacter estunensis."; RL Biologia 66:221-228(2011). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. CC A damage recognition complex composed of 2 UvrA and 2 UvrB subunits CC scans DNA for abnormalities. When the presence of a lesion has been CC verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000256|SAAS:SAAS00571360}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000256|SAAS:SAAS00571359}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00089096}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family. CC {ECO:0000256|SAAS:SAAS00571366}. 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; FN597255; CBI12145.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004602; UvrA. DR Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434, KW ECO:0000256|SAAS:SAAS00461349}; Cytoplasm {ECO:0000256|SAAS:SAAS00461486}; KW DNA damage {ECO:0000256|SAAS:SAAS00461370}; KW DNA excision {ECO:0000256|SAAS:SAAS00461384}; KW DNA repair {ECO:0000256|SAAS:SAAS00089139}; KW DNA-binding {ECO:0000256|SAAS:SAAS00461351}; KW Excision nuclease {ECO:0000256|SAAS:SAAS00461435}; KW Metal-binding {ECO:0000256|SAAS:SAAS00461425}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434, KW ECO:0000256|SAAS:SAAS00461357}; Plasmid {ECO:0000313|EMBL:CBI12145.1}; KW Repeat {ECO:0000256|SAAS:SAAS00461462}; KW Zinc {ECO:0000256|SAAS:SAAS00461396}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00461452}. FT DOMAIN 99..429 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT NP_BIND 132..139 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" SQ SEQUENCE 432 AA; 47180 MW; DC021FA0DA46B049 CRC64; MYVLDEPSIG LHQRDNERLL GTLIHLRDLG NTVIVVEHDE DAIRAADHVI DIGPGAGVHG GEVVAEGPLE AIMAVPESLT GQYMSGKRKI EVPKKRVPAN PEKVLKLTGA RGNNLKDVTL TLPVGLFTCI TGVSGSGKST LINDTLFPIA QRQLNGATIA EPAPYRDIQG LEHFDKVIDI DQSPIGRTPR SNPATYTGVF TPVRELFAGV PESRARGYTP GRFSFNVRGG RCEACQGDGV IKVRCTFLPD ILRAWRQCKV KRYNRETLEI KYKGKTIHEV LDMTIEEARE FFDAVPALAR KLQTLMVVGL TYIRLGQSAT TLSGGEAQRV KLARELSKRG TGQTLYILDE PTTGLHFADI QQLLDVLHKL RDQGNTIVVI EHNLDVIKTA DWIVDLGPEG GSGGGEILVS GTPETVAECE ASHTARFLKP ML //