ID W0JN80_9EURY Unreviewed; 379 AA.
AC W0JN80;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=HALLA_16560 {ECO:0000313|EMBL:AHG00171.1};
OS Halostagnicola larsenii XH-48.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG00171.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHG00171.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHG00171.1,
RC ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) 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 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:0000256|HAMAP-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:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000941, ECO:0000256|HAMAP-
CC Rule:MF_00099};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099}.
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}.
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DR EMBL; CP007055; AHG00171.1; -; Genomic_DNA.
DR AlphaFoldDB; W0JN80; -.
DR STRING; 797299.HALLA_16560; -.
DR KEGG; hlr:HALLA_16560; -.
DR PATRIC; fig|797299.3.peg.2319; -.
DR eggNOG; arCOG02382; Archaea.
DR HOGENOM; CLU_000445_51_0_2; -.
DR OrthoDB; 2857at2157; -.
DR Proteomes; UP000019024; 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; cd16432; CheB_Rec; 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 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 3..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 184..372
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT REGION 125..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 223
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 379 AA; 39663 MW; CD8D4B7E3A77B145 CRC64;
MVTVGIVDDS AFMRNILTEI IEQRGHEVVG EASDGESAVE LVENTNVEVI TMDISMPGQG
GHWAVDKIME RHPVPIVVLS AHVHEDAEEA LELMERGVVD IIRKPGGKER SVSLWDRADE
VVERIAGASQ SSPRSGSTID SASGSATRGA DAGATSRAGR SGSRERSALG SSSRAGSSPT
DSIESAKTTT LLVGSSTGGP DTVETLLANL PTGLDLRVLV VQHMTDALTG SFANRLDAAT
DLEFREAGAN ETITAGEGVL AKGGYHLEVT GYRRGRIDID LSKAPKINNV RPAVDATMRT
AADVIDDHMI GVILTGMGQD GAVGIKSVAD AGGRTIAQDE ATSRIFGMPK AAIETGSIEQ
VLAIDDIPDA IVRLCTDDD
//
