UVRA_STAAR
ID UVRA_STAAR Reviewed; 948 AA.
AC Q6GIN2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SAR0813;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39823.1; -; Genomic_DNA.
DR RefSeq; WP_000662687.1; NC_002952.2.
DR AlphaFoldDB; Q6GIN2; -.
DR SMR; Q6GIN2; -.
DR KEGG; sar:SAR0813; -.
DR HOGENOM; CLU_001370_0_2_9; -.
DR OMA; PFEGIIP; -.
DR OrthoDB; 152379at2; -.
DR Proteomes; UP000000596; 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; 3.40.50.300; -; 3.
DR HAMAP; MF_00205; UvrA; 1.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
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_0000093092"
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; 105367 MW; 001884D5760A0474 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 NYYKNINLSE 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
