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 27-MAR-2024, entry version 151.
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; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC 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.TM_0408; -.
DR PaxDb; 243274-THEMA_02685; -.
DR EnsemblBacteria; AAD35493; AAD35493; TM_0408.
DR KEGG; tma:TM0408; -.
DR eggNOG; COG2201; Bacteria.
DR InParanoid; Q9WYN9; -.
DR OrthoDB; 9793421at2; -.
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 CDD; cd16351; CheB_like; 1.
DR CDD; cd17541; REC_CheB-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 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 PANTHER; PTHR42872; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 1.
DR PANTHER; PTHR42872:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 1.
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; CheY-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 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
//
