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CHEB_PECAS
ID   CHEB_PECAS              Reviewed;         350 AA.
AC   Q6D6I7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 113.
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};
DE   AltName: Full=CheB_Pec {ECO:0000303|PubMed:33187094};
GN   Name=cheB {ECO:0000255|HAMAP-Rule:MF_00099}; OrderedLocusNames=ECA1693;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2] {ECO:0007744|PDB:6YMZ}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, DOMAIN, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=33187094; DOI=10.3390/ijms21228459;
RA   Velando F., Gavira J.A., Rico-Jimenez M., Matilla M.A., Krell T.;
RT   "Evidence for pentapeptide-dependent and independent CheB
RT   methylesterases.";
RL   Int. J. Mol. Sci. 21:0-0(2020).
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 (By
CC       similarity). Does not interact with the C-terminal pentapeptide of the
CC       chemoreceptors (PubMed:33187094). {ECO:0000255|HAMAP-Rule:MF_00099,
CC       ECO:0000269|PubMed:33187094}.
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. Domains are connected by a
CC       linker of approximately 25 amino acids (PubMed:33187094). The
CC       structural disorder in the region homologous to the pentapeptide-
CC       binding site in E.coli may be related to the failure to bind
CC       pentapeptides (PubMed:33187094). {ECO:0000269|PubMed:33187094}.
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   -!- DISRUPTION PHENOTYPE: Mutant does not mediate chemotaxis towards
CC       casamino acids. {ECO:0000269|PubMed:33187094}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00099}.
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DR   EMBL; BX950851; CAG74599.1; -; Genomic_DNA.
DR   RefSeq; WP_011093272.1; NC_004547.2.
DR   PDB; 6YMZ; X-ray; 2.30 A; A/B/C/D/E=1-350.
DR   PDBsum; 6YMZ; -.
DR   AlphaFoldDB; Q6D6I7; -.
DR   SMR; Q6D6I7; -.
DR   STRING; 218491.ECA1693; -.
DR   EnsemblBacteria; CAG74599; CAG74599; ECA1693.
DR   GeneID; 57209594; -.
DR   KEGG; eca:ECA1693; -.
DR   PATRIC; fig|218491.5.peg.1720; -.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_000445_51_0_6; -.
DR   OMA; MLEMHRA; -.
DR   OrthoDB; 1655418at2; -.
DR   Proteomes; UP000007966; 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   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..350
FT                   /note="Protein-glutamate methylesterase/protein-glutamine
FT                   glutaminase"
FT                   /id="PRO_0000225460"
FT   DOMAIN          5..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   DOMAIN          153..345
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           13..24
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          29..37
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           87..99
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           113..132
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          233..240
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          243..249
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           261..271
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           289..297
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           315..322
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           331..333
FT                   /evidence="ECO:0007829|PDB:6YMZ"
FT   HELIX           334..344
FT                   /evidence="ECO:0007829|PDB:6YMZ"
SQ   SEQUENCE   350 AA;  37998 MW;  D44548BA0F7AD6CB CRC64;
     MSKIRVLCVD DSALMRQIMT EIINSHPDME VVATAPDPLV ARDLIKKFNP QVLTLDVEMP
     RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EITLRALELG AIDFVTKPQL GIREGMLAYS
     ELIAEKIRMA AKARLPQRST TAEPTKIIQH MPLLSSEKLI AIGASTGGTE AIRHVLQPLP
     PTSPALLITQ HMPPGFTKSF AERLNKLCQI TVKEAEDGER VLPGHAYIAP GARHLELARS
     GANYQVRLND GPPVNRHRPS VDVLFRSVAQ YAGRNAVGVI LTGMGNDGAA GMLELHQAGA
     YTLAQNEASC VVFGMPREAI AMGGVDEVVD LHQVSQRMLA QISAGQALRI
 
 
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