UVRA_PSEPK
ID UVRA_PSEPK Reviewed; 944 AA.
AC Q88QK7;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=PP_0483;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(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; AE015451; AAN66113.1; -; Genomic_DNA.
DR RefSeq; NP_742649.1; NC_002947.4.
DR RefSeq; WP_010951778.1; NC_002947.4.
DR AlphaFoldDB; Q88QK7; -.
DR SMR; Q88QK7; -.
DR STRING; 160488.PP_0483; -.
DR PRIDE; Q88QK7; -.
DR EnsemblBacteria; AAN66113; AAN66113; PP_0483.
DR KEGG; ppu:PP_0483; -.
DR PATRIC; fig|160488.4.peg.515; -.
DR eggNOG; COG0178; Bacteria.
DR HOGENOM; CLU_001370_0_2_6; -.
DR OMA; PFEGIIP; -.
DR PhylomeDB; Q88QK7; -.
DR BioCyc; PPUT160488:G1G01-530-MON; -.
DR Proteomes; UP000000556; 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; 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; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..944
FT /note="UvrABC system protein A"
FT /id="PRO_0000093080"
FT DOMAIN 309..586
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 606..936
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 253..280
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT ZN_FING 739..765
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT BINDING 31..38
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 944 AA; 104379 MW; B6E2345CA4285981 CRC64;
MDKILIRGAR THNLKNIDLT LPRDKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
ARQFLSMMEK PDVDTIEGLS PAISIEQKST SHNPRSTVGT ITEIYDYLRL LYARVGTPRC
PDHDIPLEAQ TISQMVDLVL ERPEGSKLML LAPVVRERKG EHLAVFDELR AQGFVRARVN
GKLYELDELP KLDKQKKHSI DVVVDRFKVR ADLQQRLAES FETALKLADG IALVAPMDDE
QGEETIFSAR FACPVCGHAI SELEPKLFSF NNPAGACPTC DGLGVKQFFD TKRLVNTELT
LAEGAIRGWD RRNVYYFQML GSLAAHYGFS LEEPFGELSA EHQKVILQGS GKQSVDFKYL
NDRGDIVKRS HPFEGIVPNL ERRYRETESA TVREELAKFL GTQPCPDCRG TRLRREARHV
WVGEKTLPAV TNLPIGEASN YFGQLTLTGR RGEIAAKILK EICERLQFLV NVGLDYLTLD
RSADTLSGGE AQRIRLASQI GAGLVGVMYI LDEPSIGLHQ RDNDRLLATL NHLRDLGNTV
IVVEHDEDAI RLADYVVDIG PGAGVHGGQI VAEGSPQEVM DHPDSLTGKY LSGRKKIVVP
AKRTPRNKKL QLKLKGARGN NLQNVDLEVP IGLLTCVTGV SGSGKSTLIN NTLYPLAATA
LNGASSLEAA PHSSMDGLQH LDKVVDIDQS PIGRTPRSNP ATYTGIFTPI RELFSGVPES
RSRGYGPGRF SFNVKGGRCE ACQGDGLIKV EMHFLPDIYV PCDVCKSKRY NRETLEIKYK
GKNIHEVLEM TIEDAREFFD AVPALARKLQ TLMDVGLSYI KLGQSATTLS GGEAQRVKLS
RELSKRDTGK TLYILDEPTT GLHFADIQQL LDVLHRLRDH GNTVVVIEHN LDVIKTADWL
VDLGPEGGSK GGQIIACGTP EELSEMKQSY TGHYLKPLLE RDRA
