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UVRA_STRP1
ID   UVRA_STRP1              Reviewed;         942 AA.
AC   Q99Y84; Q48WV7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 146.
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};
GN   OrderedLocusNames=SPy_1825, M5005_Spy1550;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ52168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004092; AAK34548.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52168.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_269827.1; NC_002737.2.
DR   AlphaFoldDB; Q99Y84; -.
DR   SMR; Q99Y84; -.
DR   STRING; 1314.HKU360_01600; -.
DR   PaxDb; Q99Y84; -.
DR   EnsemblBacteria; AAK34548; AAK34548; SPy_1825.
DR   KEGG; spy:SPy_1825; -.
DR   KEGG; spz:M5005_Spy1550; -.
DR   PATRIC; fig|160490.10.peg.1585; -.
DR   HOGENOM; CLU_001370_0_2_9; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000000750; 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:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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..942
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093102"
FT   DOMAIN          308..589
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          609..937
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         251..278
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"
FT   CONFLICT        428
FT                   /note="T -> P (in Ref. 2; AAZ52168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   942 AA;  103970 MW;  FCA4B28CDCE76C90 CRC64;
     MQNKIIIHGA RAHNLKNIDV EIPRDKLVVV TGLSGSGKSS LAFDTIYAEG QRRYVESLSA
     YARQFLGNME KPDVDSIDGL SPAISIDQKT TSKNPRSTVG TVTEINDYLR LLYARVGTPY
     CINGHGAITA SSAEQIVEQV LALPERTRMQ ILAPVVRRKK GQHKTVFEKI QKDGYVRVRV
     DGDIFDVTEV PELSKSKMHN IEVVIDRLVN KDGIRSRLFD SVEAALRLGD GYLMIDTMDG
     NELLFSEHYS CPVCGFTVPE LEPRLFSFNA PFGSCPTCDG LGIKLEVDLD LVVPDPSKSL
     REGALAPWNP ISSNYYPTML EQAMASFGVD MDTPFEALTE EERDLVLYGS GDREFHFHYV
     NDFGGERNID IPFEGVVTNV NRRYHETNSD YTRNVMRGYM NELTCATCHG YRLNDQALCV
     HVGGEEGTHI GQISELSIAD HLQLLEELEL TENESTIAKP IVKEIHDRLT FLNNVGLNYL
     TLSRAAGTLS GGESQRIRLA TQIGSNLSGV LYILDEPSIG LHQRDNDRLI ESLKKMRDLG
     NTLIVVEHDE DTMMQADWLI DVGPGAGEFG GEITASGTPK QVAKNKKSIT GQYLSGKKFI
     PVPLERRSGN GRFIEIKGAA QNNLQSLDVR FPLGKFIAVT GVSGSGKSTL VNSILKKAVA
     QKLNRNADKP GKYHSISGIE HIERLIDIDQ SPIGRTPRSN PATYTGVFDD IRDLFAQTNE
     AKIRGYKKGR FSFNVKGGRC EACSGDGIIK IEMHFLPDVY VPCEVCHGRR YNSETLEVHY
     KGKNIAEVLD MTVDDALVFF SAIPKIARKI QTIKDVGLGY VTLGQPATTL SGGEAQRMKL
     ASELHKRSTG KSLYILDEPT TGLHTDDIAR LLKVLERFVD DGNTVLVIEH NLDVIKSADH
     IIDLGPEGGD GGGQIVATGT PEEVAQVKES YTGHYLKVKL QQ
 
 
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