UVRA_HELPY
ID UVRA_HELPY Reviewed; 935 AA.
AC P56474;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=HP_0705;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07755.1; -; Genomic_DNA.
DR PIR; A64608; A64608.
DR RefSeq; NP_207499.1; NC_000915.1.
DR RefSeq; WP_010875529.1; NC_000915.1.
DR AlphaFoldDB; P56474; -.
DR SMR; P56474; -.
DR DIP; DIP-3159N; -.
DR IntAct; P56474; 27.
DR MINT; P56474; -.
DR STRING; 85962.C694_03630; -.
DR PaxDb; P56474; -.
DR PRIDE; P56474; -.
DR EnsemblBacteria; AAD07755; AAD07755; HP_0705.
DR KEGG; hpy:HP_0705; -.
DR PATRIC; fig|85962.8.peg.736; -.
DR eggNOG; COG0178; Bacteria.
DR OMA; PFEGIIP; -.
DR PhylomeDB; P56474; -.
DR Proteomes; UP000000429; 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; Reference proteome;
KW Repeat; SOS response; Zinc; Zinc-finger.
FT CHAIN 1..935
FT /note="UvrABC system protein A"
FT /id="PRO_0000093054"
FT DOMAIN 310..579
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT DOMAIN 599..931
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 731..757
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 631..638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ SEQUENCE 935 AA; 104061 MW; 6ACF1A675999E141 CRC64;
MDKIIIQGAR ENNLKNIFLE IPKNQFVVFT GLSGSGKSTL AFDTLYAEGQ RRYLESLSSY
ARQFLDKVGK PNVDKIEGLT PAIAIDQKTT SKNPRSTVGT ITEIYDYLRL LFARVGEQFC
PTCLEPISSM STSDIISQIC HLEENSKIII LAPIIKDKKG SFNDKLESLR LKGYVRAFVD
GVMVRLDEEI HLHKTKKHTI EAVVDRVVVN NENASRIASA IEKALKESYG ELEVEILQDN
APSIRKHYSE HKACFKCKMS FEELEPLSFS FNSPKGACES CLGLGTKFSL DISKILDPNT
PLNQGAIKVI FGYNRSYYAQ MFEGFCEYNG IDSALCFNEL NKEQQDALLY GNGTEISFHF
KNSPLKRPWK GIIQIAYDMF KEQKDLSDYM SEKTCSSCEG HRLKASSLSV QVAGLKMADF
LTKPIEEVYH FFNDPTHFSY LNEQEKKIAE PILKEILERV FFLYDVGLGY LTLGRDARTI
SGGESQRIRI ASQIGSGLTG VLYVLDEPSI GLHEKDTLKL INTLRNLQKK GNTLIVVEHD
KETIKHADFV VDIGPKAGRH GGEVVFSGSV KELLQNNHST ALYLNGTKKI ERPKFELPKE
KHFLEIKNVN INNIKNLSVQ IPLKQLVCIT GVSGSGKSSL ILQTLLPTAQ TLLNHAKKTQ
SLNGVEIVGL EHLDKVIYLD QAPIGKTPRS NPATYTGVMD EIRILFAEQK EAKILGYSAS
RFSFNVKGGR CEKCQGDGDI KIEMHFLPDV LVQCDSCKGA KYNPQTLEIK VKGKSIADVL
NMSVEEAYEF FAKFPKIAVK LKTLMDVGLG YITLGQNATT LSGGEAQRIK LAKELSKKDT
GKTLYILDEP TTGLHFEDVN HLLQVLHSLV ALGNSMLVIE HNLDIIKNAD YIIDMGPDGG
DKGGKVIASG TPLEVAQNCE KTQSYTGKFL ALELK
