(data stored in SCRATCH zone)

SWISSPROT: B2UHV8_RALPJ

ID   B2UHV8_RALPJ            Unreviewed;       222 AA.
AC   B2UHV8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Protein phosphatase CheZ {ECO:0000256|PIRNR:PIRNR002884};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR002884};
DE   AltName: Full=Chemotaxis protein CheZ {ECO:0000256|PIRNR:PIRNR002884};
GN   OrderedLocusNames=Rpic_4056 {ECO:0000313|EMBL:ACD29159.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29159.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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:0000256|PIRNR:PIRNR002884}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR002884}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR002884}.
CC   -!- SIMILARITY: Belongs to the CheZ family.
CC       {ECO:0000256|PIRNR:PIRNR002884}.
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DR   EMBL; CP001069; ACD29159.1; -; Genomic_DNA.
DR   RefSeq; WP_004627757.1; NC_010678.1.
DR   STRING; 402626.Rpic_4056; -.
DR   EnsemblBacteria; ACD29159; ACD29159; Rpic_4056.
DR   GeneID; 6285392; -.
DR   KEGG; rpi:Rpic_4056; -.
DR   PATRIC; fig|402626.5.peg.300; -.
DR   eggNOG; ENOG4108KCC; Bacteria.
DR   eggNOG; COG3143; LUCA.
DR   HOGENOM; HOG000254724; -.
DR   KO; K03414; -.
DR   OMA; GPQIHAD; -.
DR   OrthoDB; 1206193at2; -.
DR   BioCyc; RPIC402626:GH94-4055-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
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;
DR   PRODOM; B2UHV8.
DR   SWISS-2DPAGE; B2UHV8.
KW   Chemotaxis {ECO:0000256|PIRNR:PIRNR002884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002884};
KW   Flagellar rotation {ECO:0000256|PIRNR:PIRNR002884};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR002884};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR002884};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   SITE        154    154       Enhances dephosphorylation of CheY-P.
FT                                {ECO:0000256|PIRSR:PIRSR002884-1}.
SQ   SEQUENCE   222 AA;  24642 MW;  9517573C8D729C53 CRC64;
     MSEMHDGAQA LAAEGVDHGD MPEMLQRIGH LTRMLRESMR ELGLDKGVEK AASAIPDARD
     RLNYIANMTE QAATRVLNAI DAARPVQDAL ESDSQALVNR WQSWMDRQLG DDEIRELVGQ
     TNGFLRSVPE KTRDTNQQLM EILMAQDFQD LTGQVIKKVL DVVQLIESQL VGILLDNAPE
     HLRVEAAQVA TSLLNGPQIN PDHPDVVANQ EQVDDLLESL GF
//

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