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CHEB_METMP
ID   CHEB_METMP              Reviewed;         365 AA.
AC   P62647;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000255|HAMAP-Rule:MF_00099};
DE            EC=3.1.1.61 {ECO:0000255|HAMAP-Rule:MF_00099};
DE            EC=3.5.1.44 {ECO:0000255|HAMAP-Rule:MF_00099};
GN   Name=cheB {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=MMP0926;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC       transduction system that modulates chemotaxis in response to various
CC       stimuli. Catalyzes the demethylation of specific methylglutamate
CC       residues introduced into the chemoreceptors (methyl-accepting
CC       chemotaxis proteins or MCP) by CheR. Also mediates the irreversible
CC       deamidation of specific glutamine residues to glutamic acid.
CC       {ECO:0000255|HAMAP-Rule:MF_00099}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC         glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00099};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC         Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00099};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099}.
CC   -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC       region which modulates catalytic activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00099}.
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC       regulatory domain activates the methylesterase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00099}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00099}.
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DR   EMBL; BX950229; CAF30482.1; -; Genomic_DNA.
DR   RefSeq; WP_011170870.1; NC_005791.1.
DR   AlphaFoldDB; P62647; -.
DR   SMR; P62647; -.
DR   STRING; 267377.MMP0926; -.
DR   EnsemblBacteria; CAF30482; CAF30482; MMP0926.
DR   GeneID; 2761703; -.
DR   KEGG; mmp:MMP0926; -.
DR   PATRIC; fig|267377.15.peg.954; -.
DR   eggNOG; arCOG02382; Archaea.
DR   HOGENOM; CLU_000445_51_0_2; -.
DR   OMA; MLEMHRA; -.
DR   OrthoDB; 35919at2157; -.
DR   BioCyc; MMAR267377:MMP_RS04805-MON; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   GO; GO:0018277; P:protein deamination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006482; P:protein demethylation; IEA:UniProtKB-UniRule.
DR   CDD; cd16432; CheB_Rec; 1.
DR   Gene3D; 3.40.50.180; -; 1.
DR   HAMAP; MF_00099; CheB_chemtxs; 1.
DR   InterPro; IPR008248; CheB-like.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..365
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase"
FT                   /id="PRO_0000158055"
FT   DOMAIN          5..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          177..363
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   REGION          146..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ   SEQUENCE   365 AA;  39791 MW;  8D38A9004BFBB2F7 CRC64;
     MSKIKVLIVD DSAFMRKVLE DILKSDDEIE VVATAKDGKE AFELVKKLEP NVITMDVEMP
     IMNGIDATKQ IMAYKPTPIL MLSAVTKQGS EATLKALDNG AVDFIEKPSG SVSLDIRKIG
     EKIIKQVKDA SKSKVRIKSS RILENIKKEK QDESSTPKPQ VEKTSGLSPE KLNDTAILIG
     SSTGGPPVVS SIISNIPKNT PPIFIVQHMP KGFTRVFAER MNNNSAITVK EAEHGEIVKP
     DHAYVAPGDS QMVLQKRGGN VYIIIDENMP KIHGTKPTVD VTAEYVTKYY GKNTIGVLLT
     GIGRDGANGL KMVKNKGGYT IAQNQDTCVI YGMPKTAIEM NVVDKVMDPI DIPLEIIKFA
     KKIGG
 
 
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