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CHEZ_BURM1
ID   CHEZ_BURM1              Reviewed;         243 AA.
AC   A9AD42;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=Bmul_0172, BMULJ_03092;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in bacterial chemotaxis signal
CC       transduction pathway by accelerating the dephosphorylation of
CC       phosphorylated CheY (CheY-P). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR   EMBL; CP000868; ABX13867.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44967.1; -; Genomic_DNA.
DR   RefSeq; WP_012212516.1; NC_010804.1.
DR   AlphaFoldDB; A9AD42; -.
DR   SMR; A9AD42; -.
DR   STRING; 395019.Bmul_0172; -.
DR   EnsemblBacteria; BAG44967; BAG44967; BMULJ_03092.
DR   KEGG; bmj:BMULJ_03092; -.
DR   KEGG; bmu:Bmul_0172; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_0_0_4; -.
DR   OMA; EGPQIHA; -.
DR   Proteomes; UP000008815; Chromosome 1.
DR   GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0050920; P:regulation of chemotaxis; IEA:InterPro.
DR   InterPro; IPR007439; Chemotax_Pase_CheZ.
DR   Pfam; PF04344; CheZ; 1.
DR   PIRSF; PIRSF002884; CheZ; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytoplasm; Flagellar rotation; Hydrolase; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..243
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410774"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            160
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  26577 MW;  01D8C01126BBDAA8 CRC64;
     MNEPIHAGPG DAPFGGDSQP EGADLASDRI LARIGQLTRT LRDSMRELGL DKHVERAAEA
     VPDARDRLRY VATMTEQAAE RVLNAIEIAK PVQERVQNEA EALDARWAQW YAAPIEHAEV
     RELMDDTRAF LRALPDATSA TNAQLLEIML AQDFQDLTGQ VIKKIMDMVY LIEQQLLTVL
     VENIAPERRE QFAATAAALA AEKTSATGSP ESLLNGPQIA PEGKPDVVQD QAQVDDLLAS
     LGF
 
 
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