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CHEB_THEMA
ID   CHEB_THEMA              Reviewed;         344 AA.
AC   Q9WYN9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 144.
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=TM_0408;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35493.1; -; Genomic_DNA.
DR   PIR; F72380; F72380.
DR   RefSeq; NP_228218.1; NC_000853.1.
DR   RefSeq; WP_004083251.1; NZ_CP011107.1.
DR   PDB; 3SFT; X-ray; 2.15 A; A=156-344.
DR   PDB; 3T8Y; X-ray; 1.90 A; A/B=1-144.
DR   PDBsum; 3SFT; -.
DR   PDBsum; 3T8Y; -.
DR   AlphaFoldDB; Q9WYN9; -.
DR   SMR; Q9WYN9; -.
DR   STRING; 243274.THEMA_02685; -.
DR   EnsemblBacteria; AAD35493; AAD35493; TM_0408.
DR   KEGG; tma:TM0408; -.
DR   eggNOG; COG2201; Bacteria.
DR   InParanoid; Q9WYN9; -.
DR   OMA; MLEMHRA; -.
DR   OrthoDB; 1655418at2; -.
DR   Proteomes; UP000008183; 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   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   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..344
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase"
FT                   /id="PRO_0000158032"
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          154..344
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          80..87
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           93..100
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           116..121
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   HELIX           122..132
FT                   /evidence="ECO:0007829|PDB:3T8Y"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           169..173
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           199..209
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          211..216
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          235..242
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           263..274
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          278..282
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           291..299
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          313..316
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           317..323
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   STRAND          328..331
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           333..335
FT                   /evidence="ECO:0007829|PDB:3SFT"
FT   HELIX           336..343
FT                   /evidence="ECO:0007829|PDB:3SFT"
SQ   SEQUENCE   344 AA;  37623 MW;  419C1E09B2267E55 CRC64;
     MTDRVIRVLV VDDSAFMRMV LKDIIDSQPD MKVVGFAKDG LEAVEKAIEL KPDVITMDIE
     MPNLNGIEAL KLIMKKAPTR VIMVSSLTEE GAAITIEALR NGAVDFITKP HGSISLTFRQ
     VAPELLEKIR QAMNVDPRTL LFKPKVSRLT ITKPAVSGKI VVIGSSTGGP RSLDMIIPNL
     PKNFPAPIVV VQHMPPGFTK SLAMRLDSTS ELTVKEAEDG EEVKPGFVYI APGDFHLGLK
     AQNGKVFFFL DKSDKINNVR PAVDFTLDKA AEIYKSKTIA VILTGMGKDG TKGAFKVKFY
     GGTVIAEDKE TCVVFGMPKS VIEEGYADYV LPAYKIPEKL IELV
 
 
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