ID A0A2M8WWV6_9BURK Unreviewed; 1022 AA. AC A0A2M8WWV6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, entry version 2. DE RecName: Full=UvrABC system protein A {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00385002}; DE Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000256|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205}; GN ORFNames=CLU85_0120 {ECO:0000313|EMBL:PJI95413.1}; OS Acidovorax sp. 69. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=2035202 {ECO:0000313|EMBL:PJI95413.1, ECO:0000313|Proteomes:UP000228649}; RN [1] {ECO:0000313|EMBL:PJI95413.1, ECO:0000313|Proteomes:UP000228649} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=69 {ECO:0000313|EMBL:PJI95413.1, RC ECO:0000313|Proteomes:UP000228649}; RA Chistoserdova L.; RT "Synthetic bacterial communities of pure cultures isolated from RT sediment of Lake Washington, USA."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding CC protein. A damage recognition complex composed of 2 UvrA and 2 CC UvrB subunits scans DNA for abnormalities. When the presence of a CC lesion has been verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00571360}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00571359}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00385027}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00571366}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PJI95413.1}. 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; PGEP01000001; PJI95413.1; -; Genomic_DNA. DR Proteomes; UP000228649; Unassembled WGS sequence. DR HAMAP; MF_00205; UvrA; 1. 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; 3. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|PROSITE- KW ProRule:PRU00434, ECO:0000256|SAAS:SAAS00089089}; KW Complete proteome {ECO:0000313|Proteomes:UP000228649}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00089055}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088992}; KW DNA excision {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088971}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461409}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088984}; KW Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00089033}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088968}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00089112}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088976}; KW SOS response {ECO:0000256|HAMAP-Rule:MF_00205}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00089006}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00088978}. FT DOMAIN 24 622 ABC transporter. {ECO:0000259|PROSITE: FT PS50893}. FT DOMAIN 679 1014 ABC transporter. {ECO:0000259|PROSITE: FT PS50893}. FT NP_BIND 56 63 ATP. {ECO:0000256|HAMAP-Rule:MF_00205, FT ECO:0000256|PROSITE-ProRule:PRU00434}. FT ZN_FING 280 307 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_00205}. FT NP_BIND 714 721 ATP. {ECO:0000256|HAMAP-Rule:MF_00205, FT ECO:0000256|PROSITE-ProRule:PRU00434}. FT ZN_FING 817 843 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_00205}. SQ SEQUENCE 1022 AA; 112153 MW; 166FC4C990CA090A CRC64; MTLPPVADDR SAQADDGIYL ARALREQRIS IRGARTHNLK NIDLDIPRNQ LVVITGLSGS GKSSLAFDTL YAEGQRRYVE SLSAYARQFL GRLDKPDVDL IEGLSPAISI EQKATSHNPR STVGTVTEIH DYLRLLYARA GTPYCPDHGL PLAAQTVSQM VDAVLALPED TKLMLLAPVA REKKGEFTEL FAQMQALGYI RFRVDGQIYE HENLPALKKT EKHNIDVVID RIKVRADLQQ RLAESIEAVL RVGGHEGNGR VLALEMDTGQ EHLFSSKFSC PVCSYSLPEL EPRLFSFNSP MGACPACDGI GQRDVFDPAR VVAFPTLSLA SGAIKGWDRR NGYYFAMLES LAKHYAFDID APFESLPASV QHAILHGSGD EEIAFSYIMD SGASKGKVHT KKHPFEGIIP NMARRYRETD SVVVREDLAR FRSTQPCPEC HGTRLRREAR HVRLGEGEQA RAIYEVSHAT LNTAHAWFND LKLTGAKAEI ADKVVREIAT RLQFLNDVGL SYLSLDRSAE TLSGGEAQRI RLASQIGSGL TGVMYVLDEP SIGLHQRDND RLIATLKHLR DIGNSVIVVE HDEDMMRAAD HVIDMGPGAG VHGGRVMAQG TYDEVRNNAQ SLTGQYLSGT RTIAVPTRRT PWLPVLDQPA PVVEAKAKSR FPQTEASKRR AERMAEHHAR QGAVQALRVV GATGNNLKGV TVDFPVGLLT CVTGVSGSGK STLVNDTLYT AVARQLYRAH EEPAEHEEIV GIEYFDKVIN VDQSPIGRTP RSNPATYTGL FTPIRELMAE VNTAKERGYG PGRFSFNVSQ SAGGGRCEAC QGDGVVKVEM HFLPDVYVPC DICHGQRYNR ETLEVLWKGK NIAQILELTV EDAAAYFKDV PTIARKLQTL LDVGLSYIRL GQAATTLSGG EAQRVKLAQE LSKRDTGRTL YILDEPTTGL HFADIDLLLK VLHQLRDAGN TIVIIEHNLD VIKTADWLID MGPEGGAGGG TVVGVGTPEE LAANPASHTG RYLAPYLRAQ FD //