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YEIR_ECOLI
ID   YEIR_ECOLI              Reviewed;         328 AA.
AC   P33030; P76444; P94761;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Zinc-binding GTPase YeiR {ECO:0000305};
DE            EC=3.6.-.-;
GN   Name=yeiR; OrderedLocusNames=b2173, JW2161;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP   285-328.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-105.
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=22511334; DOI=10.1039/c2mt20012k;
RA   Blaby-Haas C.E., Flood J.A., de Crecy-Lagard V., Zamble D.B.;
RT   "YeiR: a metal-binding GTPase from Escherichia coli involved in metal
RT   homeostasis.";
RL   Metallomics 4:488-497(2012).
CC   -!- FUNCTION: Involved in metal homeostasis. Has GTPase activity. Binds
CC       several Zn(2+) ions in vitro. {ECO:0000269|PubMed:22511334}.
CC   -!- ACTIVITY REGULATION: GTPase activity is enhanced by Zn(2+) binding.
CC       {ECO:0000269|PubMed:22511334}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=220 uM for GTP (in the absence of metal ions)
CC         {ECO:0000269|PubMed:22511334};
CC         KM=177 uM for GTP (in the presence of Ni(2+))
CC         {ECO:0000269|PubMed:22511334};
CC         KM=49 uM for GTP (in the presence of Zn(2+))
CC         {ECO:0000269|PubMed:22511334};
CC         Note=kcat is 0.19 min(-1). kcat is 0.33 min(-1) in the presence of
CC         Ni(2+). kcat is 0.32 min(-1) in the presence of Zn(2+).
CC         {ECO:0000269|PubMed:22511334};
CC   -!- SUBUNIT: Oligomerizes in the presence of Zn(2+).
CC       {ECO:0000269|PubMed:22511334}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene increases the sensitivity of
CC       E.coli to the metal chelator EDTA and sensitivity to cadmium.
CC       {ECO:0000269|PubMed:22511334}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. CobW
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAC75234.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15982.2; -; Genomic_DNA.
DR   EMBL; U00007; AAA60521.2; -; Genomic_DNA.
DR   PIR; D64986; D64986.
DR   RefSeq; NP_416678.1; NC_000913.3.
DR   RefSeq; WP_000198828.1; NZ_LN832404.1.
DR   AlphaFoldDB; P33030; -.
DR   SMR; P33030; -.
DR   BioGRID; 4260468; 318.
DR   BioGRID; 851042; 6.
DR   DIP; DIP-11929N; -.
DR   IntAct; P33030; 14.
DR   STRING; 511145.b2173; -.
DR   jPOST; P33030; -.
DR   PaxDb; P33030; -.
DR   PRIDE; P33030; -.
DR   EnsemblBacteria; AAC75234; AAC75234; b2173.
DR   EnsemblBacteria; BAA15982; BAA15982; BAA15982.
DR   GeneID; 946701; -.
DR   KEGG; ecj:JW2161; -.
DR   KEGG; eco:b2173; -.
DR   PATRIC; fig|1411691.4.peg.63; -.
DR   EchoBASE; EB2028; -.
DR   eggNOG; COG0523; Bacteria.
DR   HOGENOM; CLU_017452_1_2_6; -.
DR   InParanoid; P33030; -.
DR   OMA; WSIGWRW; -.
DR   PhylomeDB; P33030; -.
DR   BioCyc; EcoCyc:EG12104-MON; -.
DR   BioCyc; MetaCyc:EG12104-MON; -.
DR   PRO; PR:P33030; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR011629; Cbl_biosynth_CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..328
FT                   /note="Zinc-binding GTPase YeiR"
FT                   /id="PRO_0000169151"
FT   DOMAIN          241..321
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPZ1"
FT   BINDING         155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPZ1"
FT   CONFLICT        103..105
FT                   /note="DLL -> LSF (in Ref. 4; AAA60521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285..328
FT                   /note="GDDLHIETQNVAPPDSRIELISSSEADWNALQSALLKLRLATTA -> AMTC
FT                   TLKRKTLRHRTAVLS (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  36113 MW;  83C542DE4E0B4DA6 CRC64;
     MTRTNLITGF LGSGKTTSIL HLLAHKDPNE KWAVLVNEFG EVGIDGALLA DSGALLKEIP
     GGCMCCVNGL PMQVGLNTLL RQGKPDRLLI EPTGLGHPKQ ILDLLTAPVY EPWIDLRATL
     CILDPRLLLD EKSASNENFR DQLAAADIIV ANKSDRTTPE SEQALQRWWQ QNGGDRQLIH
     SEHGKVDGHL LDLPRRNLAE LPASAAHSHQ HVVKKGLAAL SLPEHQRWRR SLNSGQGYQA
     CGWIFDADTV FDTIGILEWA RLAPVERVKG VLRIPEGLVR INRQGDDLHI ETQNVAPPDS
     RIELISSSEA DWNALQSALL KLRLATTA
 
 
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