CHEB_HALS3
ID CHEB_HALS3 Reviewed; 347 AA.
AC B0R4K0; Q48300; Q9HQW6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=OE_2416R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R1 / S9 / D2;
RX PubMed=7556066; DOI=10.1002/j.1460-2075.1995.tb00099.x;
RA Rudolph J., Tolliday N., Schmitt C., Schuster S.C., Oesterhelt D.;
RT "Phosphorylation in halobacterial signal transduction.";
RL EMBO J. 14:4249-4257(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=8636990; DOI=10.1006/jmbi.1996.0267;
RA Rudolph J., Oesterhelt D.;
RT "Deletion analysis of the che operon in the archaeon Halobacterium
RT salinarium.";
RL J. Mol. Biol. 258:548-554(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=R1 / S9;
RX PubMed=18514223; DOI=10.1016/j.jmb.2008.04.063;
RA Koch M.K., Staudinger W.F., Siedler F., Oesterhelt D.;
RT "Physiological sites of deamidation and methyl esterification in sensory
RT transducers of Halobacterium salinarum.";
RL J. Mol. Biol. 380:285-302(2008).
CC -!- FUNCTION: Involved in the modulation of the chemotaxis system;
CC catalyzes the demethylation of specific methylglutamate residues
CC introduced into the Htr transducer proteins (methyl-accepting
CC chemotaxis proteins) by CheR. Also required for Htr deamidations, at
CC least at a specific glutamine-glutamate pair in HTR-II and a specific
CC aspartate-glutamine pair in Htr4. {ECO:0000269|PubMed:18514223}.
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, ECO:0000269|PubMed:18514223};
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, ECO:0000269|PubMed:18514223};
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 -!- DISRUPTION PHENOTYPE: Deletion leads to the loss of both chemotactic
CC and phototactic responses. Mutants show increased methylation of the
CC Htr transducer proteins. {ECO:0000269|PubMed:18514223,
CC ECO:0000269|PubMed:8636990}.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; X86407; CAA60162.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP13665.1; -; Genomic_DNA.
DR PIR; S58646; S58646.
DR RefSeq; WP_010902691.1; NC_010364.1.
DR AlphaFoldDB; B0R4K0; -.
DR SMR; B0R4K0; -.
DR EnsemblBacteria; CAP13665; CAP13665; OE_2416R.
DR GeneID; 5953631; -.
DR KEGG; hsl:OE_2416R; -.
DR HOGENOM; CLU_000445_51_0_2; -.
DR OMA; MLEMHRA; -.
DR PhylomeDB; B0R4K0; -.
DR Proteomes; UP000001321; 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 Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein.
FT CHAIN 1..347
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000429068"
FT DOMAIN 3..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 152..346
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 132..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 288
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT CONFLICT 295
FT /note="A -> P (in Ref. 1; CAA60162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 36484 MW; 9691873DC8EA113B CRC64;
MTEALVVDDS HFMRTVISDI LEDGGVDVVG TAENGARALD AVTDVQPDVI TMDVEMPEMD
GIEATAEIMR EQPTPILMVS ALTTEDADAT LEAMEKGAID TFAKPGGTIS TELSGHSEEL
VAAVERVASA DPTAGHDVEM EPASPPDATT SEYADNPTLL IGASTGGPNV VESILASLPA
EADFRVLIVQ HMPDQFTSRF ADRLDAASQY DITEAEDGSR IGGGEGLVAR GDYHMRVSGY
SNGRLRVRLD QSERLHSVRP AIDVTFKSAA ERVTDPLVSV VLTGMGSDGA DGVRAVKDAG
GATLAQNEAT SAVFGIPERA IETGCVDDVL PVDQLTEAIA DSIRRTT
