ID   UVRA_STAAW              Reviewed;         948 AA.
AC   Q8NXL9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
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}; OrderedLocusNames=MW0721;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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}.
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DR   EMBL; BA000033; BAB94586.1; -; Genomic_DNA.
DR   RefSeq; WP_000662681.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXL9; -.
DR   SMR; Q8NXL9; -.
DR   EnsemblBacteria; BAB94586; BAB94586; BAB94586.
DR   KEGG; sam:MW0721; -.
DR   HOGENOM; CLU_001370_0_2_9; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000000418; 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   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00630; uvra; 1.
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..948
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093094"
FT   DOMAIN          309..587
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          607..935
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         738..764
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   948 AA;  105368 MW;  501884D576087DCF CRC64;
     MKEPSIVVKG ARAHNLKDID IELPKNKLIV MTGLSGSGKS SLAFDTIYAE GQRRYVESLS
     AYARQFLGQM DKPDVDTIEG LSPAISIDQK TTSKNPRSTV ATVTEIYDYI RLLYARVGKP
     YCPNHNIEIE SQTVQQMVDR IMELEARTKI QLLAPVIAHR KGSHEKLIED IGKKGYVRLR
     IDGEIVDVND VPTLDKNKNH TIEVVVDRLV VKDGIETRLA DSIETALELS EGQLTVDVID
     GEDLKFSESH ACPICGFSIG ELEPRMFSFN SPFGACPTCD GLGQKLTVDV DLVVPDKDKT
     LNEGAIEPWI PTSSDFYPTL LKRVCEVYKI NMDKPFKKLT ERQRDILLYG SGDKEIEFTF
     TQRQGGTRKR TMVFEGVVPN ISRRFHESPS EYTREMMSKY MTELPCETCH GKRLSREALS
     VYVGGLNIGE VVEYSISQAL NYYKNIDLSE QDQAIANQIL KEIISRLTFL NNVGLEYLTL
     NRASGTLSGG EAQRIRLATQ IGSRLTGVLY VLDEPSIGLH QRDNDRLINT LKEMRDLGNT
     LIVVEHDDDT MRAADYLVDI GPGAGEHGGQ IVSSGTPQKV MKDKKSLTGQ YLSGKKRIEV
     PEYRRPASDR KISIRGARSN NLKGVDVDIP LSIMTVVTGV SGSGKSSLVN EVLYKSLAQK
     INKSKVKPGL YDKIEGIDQL DKIIDIDQSP IGRTPRSNPA TYTGVFDDIR DVFAQTNEAK
     IRGYQKGRFS FNVKGGRCEA CKGDGIIKIE MHFLPDVYVP CEVCDGKRYN RETLEVTYKG
     KNIADILEMT VEEATQFFEN IPKIKRKLQT LVDVGLGYVT LGQQATTLSG GEAQRVKLAS
     ELHKRSTGKS IYILDEPTTG LHVDDISRLL KVLNRLVENG DTVVIIEHNL DVIKTADYII
     DLGPEGGSGG GTIVATGTPE DIAQTKSSYT GKYLKEVLER DKQNTEDK