CHEB3_CERSP
ID CHEB3_CERSP Reviewed; 369 AA.
AC O33558;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Protein-glutamate methylesterase/protein-glutamine glutaminase of group 3 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=cheB3; Synonyms=cheB1;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WS8N;
RX PubMed=9426144; DOI=10.1046/j.1365-2958.1997.6502022.x;
RA Hamblin P.A., Maguire B.A., Grishanin R.N., Armitage J.P.;
RT "Evidence for two chemosensory pathways in Rhodobacter sphaeroides.";
RL Mol. Microbiol. 26:1083-1096(1997).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=WS8N;
RX PubMed=11717272; DOI=10.1128/jb.183.24.7135-7144.2001;
RA Martin A.C., Wadhams G.H., Shah D.S.H., Porter S.L., Mantotta J.C.,
RA Craig T.J., Verdult P.H., Jones H., Armitage J.P.;
RT "CheR- and CheB-dependent chemosensory adaptation system of Rhodobacter
RT sphaeroides.";
RL J. Bacteriol. 183:7135-7144(2001).
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 in vitro by CheA2, but not by CheA1.
CC Phosphorylation of the N-terminal regulatory domain activates the
CC methylesterase activity.
CC -!- MISCELLANEOUS: R.sphaeroides does not have a cheB in its group 1
CC operon. Part of the third chemotactic pathway (cheOp3); there are 3
CC operons encoding multiple homologs of the chemosensory proteins in
CC R.sphaeroides. This locus, and cheB2, are essential for chemotaxis.
CC CheB2 is not involved in phototaxis signaling. This protein 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; AJ000977; CAA04433.1; -; Genomic_DNA.
DR PIR; T45021; T45021.
DR AlphaFoldDB; O33558; -.
DR SMR; O33558; -.
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..369
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase of group 3 operon"
FT /id="PRO_0000158025"
FT DOMAIN 11..128
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 170..358
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 209
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 305
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
SQ SEQUENCE 369 AA; 39635 MW; 5B2496EE7C895382 CRC64;
MTTHAAAPST RVLIVDDSAA ARAMFKVIVE SDPALQVMAA VPDAFAAARA MRTELPDVIL
LDLELPSMDG LTFLRKIMQQ HPIPVVVCSS HVGAGTEAMV SALELGAREV ISKPAARNDL
ERQEASIRIC DAIRAATETT RRRSQPEPRP LAPGPKLTAD EILPARPPRP VPETMPVVCI
GASTGGTEAL RDVLTALPAS APPIVIVQHM PRGFTAAFAR RLDSLCAIEV LEAEDEMQVM
PGRAIIAQGD RHLLLRRRNQ GYRVSVLDGA YVCRHRPSVD VLFRSAAQEA GGNALGVIMT
GMGDDGARCM AEMRAAGAET IAQNEESCVV YGMPREAVAH GGVGKVEPLD RLAARIMEFG
RRHTERTVR
