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UVRA_LACPL
ID   UVRA_LACPL              Reviewed;         951 AA.
AC   Q88YI7; F9ULZ7;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=lp_0773;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC78236.1; -; Genomic_DNA.
DR   RefSeq; WP_003643969.1; NC_004567.2.
DR   RefSeq; YP_004888750.1; NC_004567.2.
DR   AlphaFoldDB; Q88YI7; -.
DR   SMR; Q88YI7; -.
DR   STRING; 220668.lp_0773; -.
DR   EnsemblBacteria; CCC78236; CCC78236; lp_0773.
DR   GeneID; 57024477; -.
DR   KEGG; lpl:lp_0773; -.
DR   PATRIC; fig|220668.9.peg.653; -.
DR   eggNOG; COG0178; Bacteria.
DR   HOGENOM; CLU_001370_0_2_9; -.
DR   OMA; PFEGIIP; -.
DR   PhylomeDB; Q88YI7; -.
DR   BioCyc; LPLA220668:G1GW0-671-MON; -.
DR   Proteomes; UP000000432; 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; 2.
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..951
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093057"
FT   DOMAIN          309..587
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          607..935
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         738..764
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                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   951 AA;  104985 MW;  E7C3A91420CBB1DD CRC64;
     MANDKIVIHG ARAHNLKDID VTIPRDKLVV ITGLSGSGKS SLAFDTLYAE GQRRYVESLS
     AYARQFLGQM QKPDVDSIDG LSPAISIDQK TTSKNPRSTV GTVTEINDYL RLLWARVGEP
     ICPNDGTPIA SQTVEQMVDR IQKLPERTKL QILSPIVRQK KGEHKKIFEK IKREGFVRVR
     VDGDIHDISE TFELNKNQQH TIEIVIDRIV VKSGDRSRLF DSFEAALRLS GGYAIADVIG
     GEPIMFSEHY ACPICGFTVG ELEPRLFSFN APQGACPDCE GLGIKLEVDE DLVVPDKSLT
     LAEGALAPWN PISSQYYPEM LKQACEQLEI PMDVPYEDLS KADQQTVLYG SNGKTFHFHY
     QNDFGGVRDV DAVFEGVINN VDRRYHETNS DFTRDVMRKY MTELTCQTCH GFRLNRKALS
     VKVGGEHIGM VSDLAIGKEL DFFNELSLSE QSLVIAKPIL KEIRDRLSFL QNVGLAYLTL
     SRSARTLSGG EAQRIRLATQ IGSNLSGVLY ILDEPSIGLH QRDNDRLIGS LKKMRDLGNT
     LIVVEHDEDT MRAADYIVDI GPGAGENGGE VMAAGTPKQV ARSRKSLTGQ YLSGKRFIPL
     PETRRPGNGK KIRITGAAEN NLKQIDVDFP LGEFVVVTGV SGSGKSTLVN DVLKRVLAQK
     LNRNSEKPGK YKSVSGIKNI ERLVNIDQSP IGRTPRSNPA TYTGVFDNIR DLFAQTNEAK
     LRGYKKGRFS FNTKGGRCEA CHGDGILKIE MNFLPDVFVP CEVCHGKQYN SETLEVEYKG
     KNIADVLQMT ASEAVKFFEP IPKIRRKLQT LVDVGLGYVK LGQPATTLSG GEAQRMKLAS
     ELHKQQSGKN FYILDEPTTG LHSEDIRRLI GVLDRLVDAG NTVLIIEHNL DVVKSADYLI
     DLGPEGGDGG GTIVATGTPE QVAEVAESYT GQYLKPVLER DRAREATAPA K
 
 
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