ID UVRA_MYCPN Reviewed; 948 AA. AC P75176; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 138. 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=MPN_619; ORFNames=MP223; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB95871.1; -; Genomic_DNA. DR PIR; S73549; S73549. DR RefSeq; NP_110308.1; NC_000912.1. DR RefSeq; WP_010874976.1; NZ_OU342337.1. DR AlphaFoldDB; P75176; -. DR SMR; P75176; -. DR IntAct; P75176; 3. DR STRING; 272634.MPN_619; -. DR EnsemblBacteria; AAB95871; AAB95871; MPN_619. DR KEGG; mpn:MPN_619; -. DR PATRIC; fig|272634.6.peg.683; -. DR HOGENOM; CLU_001370_0_2_14; -. DR OrthoDB; 9809851at2; -. DR BioCyc; MPNE272634:G1GJ3-999-MONOMER; -. DR Proteomes; UP000000808; Chromosome. 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; 3. 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; Reference proteome; KW Repeat; SOS response; Zinc; Zinc-finger. FT CHAIN 1..948 FT /note="UvrABC system protein A" FT /id="PRO_0000093066" FT DOMAIN 316..595 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT DOMAIN 615..944 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT ZN_FING 259..286 FT /note="C4-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT ZN_FING 746..772 FT /note="C4-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT BINDING 38..45 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" FT BINDING 647..654 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205" SQ SEQUENCE 948 AA; 105426 MW; 4466DE773D3B370C CRC64; MKPELKTNDF IRVKGARENN LKNVNIDIPK NQFVVITGLS GSGKSSLAFN TIYAEGRRRY LESLSSYARQ FLGNSDKPDV DSIEGLSPAI SIDQKTTSHN PRSTVGTVTE IYDYLRLLWA RIGIPFCPNG HGAIQTQTVN QIANQIFNLP VKSRIQILAP TIKNQRGTFA NEFAKYQQLG FLRVWVDGQV YTLDEEIKLD KNTKHNLSVV VDRIVINQDK QTLGRIVDAI EGVIKLTEGR IEVLLEDGKI LSFNKNHGCD QCGFSISELE PRLFSFNSPL GSCEYCKGLG FSYEPDVEKI IPNPLLSINE GGIDIFKNIV HGTSLDWQRF LSLINHYQIP LDQPLGQMDT DLVRMILEGS DEPIEIKTVS NSGAKNVRFE HYEGVAHLIK RRHLETSSQA SREWYSAYMS EITCKKCQGK KLTTNSLSVK LGGLDIISFT ELSIDKAIEF LLQIELNQEQ KKIGELALKE IINRLSFLKN VGLEYLNLAR RASTLSGGEA QRIRLATQIG SQLTGVLYVL DEPSIGLHQK DNDRLINTMM VMRDLGNTLL VVEHDSETML AADYLIDIGP KAGNQGGEVV AAGTPLEVME NPDSLTGQYL SGKKQIEVPK TRHAGNGRTL TLKGAKGNNL KNINVTIPLN KLVLVTGVSG SGKSTLINQT LVPILERLVN YKNVKPAPYK EIIGVNHIDK VVVVSQDPIG RTPRSNPATY VSVFDDIREL FANTKEAKAR GYTNSRFSFN VAGGRCDKCF GDGVIRIEMH FLPDVYVTCE MCDGKKYNPQ TLEVKYLGKS IFDVLQMSCQ EAYDFFKAIP NIARKLKLLC DVGLEYLQLG LNVTFLSGGE AQRIKLAKFL QKKATGKTLY VLDEPSTGLH IEDINKLLTV IQRIIKNGDS VIIIEHNLDI IKMADYIIDL GPEGGEKGGQ IIAQGTPEQL LNQVDKSYTA QYLAKILK //