(data stored in SCRATCH zone)

SWISSPROT: A8FPM2_SHESH

ID   A8FPM2_SHESH            Unreviewed;       345 AA.
AC   A8FPM2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase {ECO:0000256|HAMAP-Rule:MF_00099};
DE            EC=3.1.1.61 {ECO:0000256|HAMAP-Rule:MF_00099};
DE            EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_00099};
GN   Name=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN   OrderedLocusNames=Ssed_0182 {ECO:0000313|EMBL:ABV34795.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34795.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34795.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34795.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal
CC       transduction system that modulates chemotaxis in response to
CC       various stimuli. Catalyzes the demethylation of specific
CC       methylglutamate residues introduced into the chemoreceptors
CC       (methyl-accepting chemotaxis proteins or MCP) by CheR. Also
CC       mediates the irreversible deamidation of specific glutamine
CC       residues to glutamic acid. {ECO:0000256|HAMAP-Rule:MF_00099,
CC       ECO:0000256|SAAS:SAAS01100814}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-
CC         COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00099,
CC         ECO:0000256|SAAS:SAAS01116312};
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:0000256|HAMAP-
CC         Rule:MF_00099, ECO:0000256|SAAS:SAAS01130167};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
CC       ECO:0000256|SAAS:SAAS00132521}.
CC   -!- DOMAIN: Contains a C-terminal catalytic domain, and an N-terminal
CC       region which modulates catalytic activity. {ECO:0000256|HAMAP-
CC       Rule:MF_00099}.
CC   -!- PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal
CC       regulatory domain activates the methylesterase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00099}.
CC   -!- SIMILARITY: Belongs to the CheB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00099, ECO:0000256|SAAS:SAAS01100824}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000821; ABV34795.1; -; Genomic_DNA.
DR   RefSeq; WP_012004321.1; NC_009831.1.
DR   STRING; 425104.Ssed_0182; -.
DR   EnsemblBacteria; ABV34795; ABV34795; Ssed_0182.
DR   KEGG; sse:Ssed_0182; -.
DR   eggNOG; ENOG4105CMP; Bacteria.
DR   eggNOG; COG2201; LUCA.
DR   HOGENOM; HOG000151424; -.
DR   KO; K03412; -.
DR   OMA; YFPKPSV; -.
DR   OrthoDB; 1655418at2; -.
DR   BioCyc; SSED425104:G1G9Y-191-MONOMER; -.
DR   Proteomes; UP000002015; 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   CDD; cd00156; 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;
DR   PRODOM; A8FPM2.
DR   SWISS-2DPAGE; A8FPM2.
KW   Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099,
KW   ECO:0000256|SAAS:SAAS00132526};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00050, ECO:0000256|SAAS:SAAS00706700,
KW   ECO:0000313|EMBL:ABV34795.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015}.
FT   DOMAIN        3    120       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      150    342       CheB-type methylesterase.
FT                                {ECO:0000259|PROSITE:PS50122}.
FT   ACT_SITE    162    162       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    188    188       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   ACT_SITE    284    284       {ECO:0000256|HAMAP-Rule:MF_00099,
FT                                ECO:0000256|PROSITE-ProRule:PRU00050}.
FT   MOD_RES      54     54       4-aspartylphosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00099, ECO:0000256|PROSITE-
FT                                ProRule:PRU00169}.
SQ   SEQUENCE   345 AA;  36942 MW;  70A5662019777D02 CRC64;
     MIKVLIVDDS PLVRQLLTHL LSDTSDISVV GAAEDPYEAR ELIKRFNPDV LTLDIEMPKM
     DGIAFLRNLM KLRPMPVVMI STLTEKGAAV TLEALSIGAV DFISKPKSDL TNKLMEYRDE
     LIEKVRFAAK SKVRPTSPIP APKLCTSPTG CSQNQLIAIG ASTGGTEAIQ RLICQLPSDV
     PPIVIAQHIP AAFSASFAKR LDSHASMRVI EAQGGELLKP GTAYIAPGSA HLIIEKRGGL
     LYTRLLDSEP VNRHKPSVDV LFDSVAETAG KSALGVILTG MGKDGAKGLL NMKQSGAYTL
     AQDEASSVVW GMPGAAVELD ANCEELHIDR IPAKLLSVMK NASQA
//

If you have problems or comments...

PBIL Back to PBIL home page