UVRA_XYLFT
ID UVRA_XYLFT Reviewed; 965 AA.
AC Q87BK9;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PD_1444;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO29288.1; -; Genomic_DNA.
DR RefSeq; WP_004088411.1; NC_004556.1.
DR AlphaFoldDB; Q87BK9; -.
DR SMR; Q87BK9; -.
DR PRIDE; Q87BK9; -.
DR EnsemblBacteria; AAO29288; AAO29288; PD_1444.
DR GeneID; 58016968; -.
DR KEGG; xft:PD_1444; -.
DR HOGENOM; CLU_001370_0_0_6; -.
DR OMA; PFEGIIP; -.
DR Proteomes; UP000002516; 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; 2.
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..965
FT /note="UvrABC system protein A"
FT /id="PRO_0000093119"
FT DOMAIN 311..588
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 608..937
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 254..281
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 740..766
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 641..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 965 AA; 106939 MW; 2C56691CDF7D506B CRC64;
MTALIRIRGA RTHNLKNLDL DLPRNTLIVI TGLSGSGKSS LAFDTIYAEG QRRYVESLSA
YARQFLSVME KPDVDHIEGL SPAISIEQKS TSHNPRSTVG TITEIYDYLR LLYARVGQPR
CPEHHYPLEA QTVSQMVDHV LTLDPEQRYM LLAPVVRERK GEHTQVFEQL RAQGFVRVRV
DGELYEIDAV PTLTLRQKHT IEAVIDRFRP REDIKQRLAE SFETALKLGN GMASVQTLDT
TTATPHLFSS KYSCPVCDYS LPELEPRLFS FNAPMGACPA CNGLGVTEFF DPAKVVIHPD
LSLSAGAVRG WDRRNAYYFQ LIASLAKHYT FDIDASWESL PEEIRHTILF GSGDEQINFT
YLTEAGGRTK RKHRFEGIVP NLERRYRETE SAAVREELAK YVSTRTCPEC GGTRLNRAAR
NVFVADRTLP ELTVLPINDA LEFFKTLRLS GWRGEIAIKI VKEIGERLGF LVDVGLDYLT
LERKADTLSG GEAQRIRLAS QIGAGLVGVM YVLDEPSIGL HQRDNERLLG TLTRLRDLGN
TVIVVEHDED AIRQADHILD IGPGAGVHGG EICAQGSLEQ IMAAPRSLTG QYLSGRRRIE
IPKQRHPPNA TKMLHLRGAC GNNLKGVNLD IPEGLFTCIT GVSGSGKSTL INDTLFTLAA
NEINGASHPI APYASVDGLE LFDKVVDIDQ SPIGRTPRSN PATYTGMFTP LRELFAQVPE
ARARGYSPGR FSFNVRGGRC EACEGDGLIK VEMHFLPDVY VPCDICHGKR YNRETLEIRY
KGYNINDVLE MTVEDALKLF EAVPAIARKL ETLVDVGLSY LKLGQSATTL SGGEAQRVKL
SKELSRRDTG HTLYILDEPT TGLHFYDIEA LLAVMHKLRD AGNTVIVIEH NLDVIKTADW
VIDLGPEGGG RGGEILVAGT PETVAAHPHS HTGHFLAKLL PPKDVSNCGH RNPKEEVDIA
KTVHR