CHEB2_CERSP
ID CHEB2_CERSP Reviewed; 366 AA.
AC Q8KLS5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase of group 2 operon;
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=cheB2 {ECO:0000255|HAMAP-Rule:MF_00099};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=WS8N;
RX PubMed=12421313; DOI=10.1046/j.1365-2958.2002.03218.x;
RA Porter S.L., Warren A.V., Martin A.C., Armitage J.P.;
RT "The third chemotaxis locus of Rhodobacter sphaeroides is essential for
RT chemotaxis.";
RL Mol. Microbiol. 46:1081-1094(2002).
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 -!- MISCELLANEOUS: R.sphaeroides does not have a cheB in its group 1
CC operon. Part of the second chemotactic pathway (cheOp2); there are 3
CC operons encoding multiple homologs of the chemosensory proteins in
CC R.sphaeroides. This protein is essential for chemotaxis, and is able to
CC partially complement an E.coli cheB deletion mutant.
CC -!- SIMILARITY: Belongs to the CheB family. {ECO:0000255|HAMAP-
CC Rule:MF_00099}.
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DR EMBL; AJ488585; CAD32756.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KLS5; -.
DR SMR; Q8KLS5; -.
DR DIP; DIP-48636N; -.
DR IntAct; Q8KLS5; 1.
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..366
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase of group 2 operon"
FT /id="PRO_0000158024"
FT DOMAIN 19..136
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 162..356
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 201
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 298
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 70
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 366 AA; 37948 MW; 60AD92C45252EB10 CRC64;
MKAAADRLMA ARAREGRTRV LIVDDSAMVR QALALGLSTD PRLEVVGTAS GAEAARAQMA
ALKPDVVTLD LEMPQMDGLT FLRSYMESAP VPTVVISSLT RTSGETAMRA MEAGAVDIIS
KPSLGAGQGL PAIMRDVCAR VWAAARARLA LPDGAAPAPV APGASEDWIH ALGASTGGVQ
ALSRILPFFP AQSPGLLVVQ HMPEGFTAAF ARRLDALCRM RVREAADGDL VLPGLVLIAP
GGLRHMEIER AGGVCRVRLV AGAPVSYSRP SVDRMFLSLA AAAGPRVSAA LLTGMGRDGA
AGLLAIRRAG GRTFAQDEGS SAVFGMPLAA RDLRAAEEIL TLDDIPARMM LAAAADTRAP
SLASND
