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UVRA_RICPR
ID   UVRA_RICPR              Reviewed;         953 AA.
AC   Q9ZCC3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=RP835;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235273; CAA15260.1; -; Genomic_DNA.
DR   PIR; D71645; D71645.
DR   RefSeq; NP_221184.1; NC_000963.1.
DR   RefSeq; WP_004596819.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCC3; -.
DR   SMR; Q9ZCC3; -.
DR   STRING; 272947.RP835; -.
DR   PRIDE; Q9ZCC3; -.
DR   EnsemblBacteria; CAA15260; CAA15260; CAA15260.
DR   GeneID; 57569958; -.
DR   KEGG; rpr:RP835; -.
DR   PATRIC; fig|272947.5.peg.872; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_5; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000002480; 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; 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..953
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093084"
FT   DOMAIN          320..599
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          619..949
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         752..778
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         652..659
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   953 AA;  106287 MW;  6209A66241379421 CRC64;
     MNQEYIKVRG AKEHNLKNIN VDIPRNKFVV ITGLSGSGKS SLAFDTIYAE GQRRYVESLS
     SYARQFLHLQ NKPNVESISG LSPAIAIDQK TTSKNPRSTV GTITEIYDYL RLLYARVGIP
     YSPVTSLPIH SQTVAEMVDI INELPKGTKV YLLAPIVRGH KGEFKREIMN LKKQGFQKLI
     VNGEVCEIDD LPKLDKNKKH NIEVIVDRIV LDENLGNRLA DSLESSLNLA DGITYLEIVE
     LPQAVKSQFE KNQRITFSEK YSCPVSGFQL TEIEPRIFSF NSPFGACPKC EGIGKEFFFD
     RDLIVQDQRI SIKDGAIVPW GSTSSKFILE TLKALADHYK FSIEVPFISL SQSVKDILFE
     GSGEEEIKFE FHDGSKTQII KQPFAGIIPS LQEKDRTIES VLIKEELAKF KSEHKCTACS
     GFRLKDEALC VKIANLHIGE VAGMSIAALQ KWFIHLEEKL NQKQLFIAKR ILKEINERLK
     FLMNVGLDYL TLSREAGTLS GGESQRIRLA SQIGSGLSGV LYVLDEPSIG LHQRDNTRLI
     ATLKRLRDLG NTVLVVEHDE ETMYEADHII DIGPGAGIHG GRVIAEGNAE KIKHFEESIT
     GRYLSGRQTI KVPSETRVGH DNRAIELLGA VSNNLDNVDI KIPLGTFTAI TGVSGSGKSS
     LMIHTLYKAA LKHLEPTSKV FPGKYRELKG LEYIDKIIDI NQSPIGRTPR SNPATYTGAF
     THIRDWFVEL PESKARGYKV GRFSFNVKGG RCEACQGDGL IKIEMHFLPD VYVKCDICNG
     HRYNRETLEI KYKGKSIADI LMMTVEDAMQ FFDKIPLIYE KLITLNEVGL GYIKIGQSAT
     TLSGGEAQRV KLAKELSRRS TGKTLYILDE PTTGLHIDDI KKLLKVLHKL VDMGNTVLVI
     EHNLDVIKTA DYIIDVGPEG GDKGGKIVVC GTPTDIAACK ESHTGRYLKQ YLI
 
 
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