ID UVRA_BRUAB Reviewed; 974 AA. AC P0C0Z2; Q07433; Q57D33; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205}; DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; GN OrderedLocusNames=BruAb1_1110; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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. {ECO:0000255|HAMAP- CC Rule:MF_00205}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family. CC {ECO:0000255|HAMAP-Rule:MF_00205}. 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; AE017223; AAX74451.1; -; Genomic_DNA. DR RefSeq; WP_002964233.1; NC_006932.1. DR AlphaFoldDB; P0C0Z2; -. DR SMR; P0C0Z2; -. DR EnsemblBacteria; AAX74451; AAX74451; BruAb1_1110. DR GeneID; 3787776; -. DR KEGG; bmb:BruAb1_1110; -. DR HOGENOM; CLU_001370_0_1_5; -. DR PRO; PR:P0C0Z2; -. DR Proteomes; UP000000540; Chromosome I. 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:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule. DR CDD; cd03270; ABC_UvrA_I; 1. DR CDD; cd03271; ABC_UvrA_II; 1. DR Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1. DR Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_00205; UvrA; 1. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004602; UvrA. DR InterPro; IPR041552; UvrA_DNA-bd. DR InterPro; IPR041102; UvrA_inter. DR NCBIfam; TIGR00630; uvra; 1. DR PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1. DR PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1. DR Pfam; PF17755; UvrA_DNA-bind; 1. DR Pfam; PF17760; UvrA_inter; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding; KW Excision nuclease; Metal-binding; Nucleotide-binding; Repeat; SOS response; KW Zinc; Zinc-finger. FT CHAIN 1..974 FT /note="UvrABC system protein A" FT /id="PRO_0000093038" FT DOMAIN 331..610 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT DOMAIN 630..959 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT ZN_FING 762..788 FT /note="C4-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT BINDING 34..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT BINDING 663..670 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" SQ SEQUENCE 974 AA; 107423 MW; 15F7C2BADB7B3127 CRC64; MSDQKFISIR GAREHNLKNV DLDLPRDKLI VMTGLSGSGK SSLAFDTIYA EGQRRYVESL SAYARQFLEM MQKPDVDQID GLSPAISIEQ KTTSRNPRST VGTVTEIYDY MRLLFARVGI PYSPATGLPI ESQTVSQMVD RVIALEEGTR LYILAPIVRG RKGEYRKELA ELQKKGFQRV KVDGTFYEIA DVPPLDKKYK HDIDVVVDRV VVRPDLSTRL ADSLETCLKL ADGLAIAEFA DKPLPVGETA EGGSANKSAN ETHERILFSE KFACPVSGFT IPEIEPRLFS FNNPFGACPT CDGLGTQQAI DPNLIIPDES AALKDGAVAP WARSSSPYYN QTLEALGKAY GFKVSARWSE LSEEARQAIL YGTKGREITF HYDDGLRSYQ TTKPFEGVIP NLERRWKETD SAWSREEIER FMASTPCPAC NGYRLKPEAL SVKIGKKHIG EITEMSIRKA DAWFRDIDGS FNEKQREIAA RILKAIRERL QFLNNVGLDY LTLARNSGTL SGGESQRIRL ASQIGSGLTG VLYVLDEPSI GLHQRDNARL LDTLRHLRDL GNTVIVVEHD EDAILTADYV VDIGPAAGVH GGKVIAQGSP QDIMANTNSL TGKYLSGAME VAVPAERRKI SKTKRLRVVG ARGNNLKNVS ADIPLGTFTA VTGVSGGGKS TFLIETLFKA ASRRIMGSRE HPAEHDRIEG LEFLDKVIDI DQSPIGRTPR SNPATYTGAF TPIRDWFAGL PEAKARGYQP GRFSFNVKGG RCEACQGDGV IKIEMHFLPD VYVTCDVCHG KRYNRETLDV LFKGKSIADV LDMTVEEGAE FFSAVPAVRD KLETLVKVGL GYIKVGQQAT TLSGGEAQRV KLAKELSRRA TGRTLYILDE PTTGLHFHDV AKLLEVLHEL VEQGNTVVVI EHNLEVIKTA DWVIDLGPEG GDGGGEIVAV GRPEDIVQEK RSYTGQFLKE LLERRPKRSS QAAE //