CHEB1_VIBPA
ID CHEB1_VIBPA Reviewed; 369 AA.
AC Q87MK5; Q9LB11;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=VP2228;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RA Jaques S., Kim Y.K., McCarter L.L.;
RT "Components of the polar flagellar switch complex and assembly apparatus.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; AF069392; AAF32418.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC60491.1; -; Genomic_DNA.
DR RefSeq; NP_798607.1; NC_004603.1.
DR RefSeq; WP_005479477.1; NC_004603.1.
DR AlphaFoldDB; Q87MK5; -.
DR SMR; Q87MK5; -.
DR STRING; 223926.28807221; -.
DR EnsemblBacteria; BAC60491; BAC60491; BAC60491.
DR GeneID; 1189741; -.
DR KEGG; vpa:VP2228; -.
DR PATRIC; fig|223926.6.peg.2131; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_6; -.
DR OMA; YGMPMAV; -.
DR Proteomes; UP000002493; Chromosome 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 3: Inferred from homology;
KW Chemotaxis; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..369
FT /note="Protein-glutamate methylesterase/protein-glutamine
FT glutaminase"
FT /id="PRO_0000158038"
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT DOMAIN 176..369
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 215
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00099"
FT CONFLICT 149
FT /note="S -> A (in Ref. 1; AAF32418)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="T -> A (in Ref. 1; AAF32418)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> M (in Ref. 1; AAF32418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 39427 MW; 13F7DA7144FE1084 CRC64;
MAIKVLVVDD SSFFRRRVSE IINSESRLEV IDVAVNGREA VEKAKALKPD VITMDIEMPV
MDGITAVREI MAASPTPILM FSSLTHDGAK ATLDALDAGA LDFLPKKFED IARNRDEAVS
LLQQRVIQIA SKRAFMRRPV ARPAAATSSA RPLASRTAAP AASAPARPAT TKFRASGKKY
QLTAIGTSTG GPVALQKILT RLPMNYPHPI VLIQHMPATF TAAFASRLNT LCKIQVKEAQ
DGDVLQAGVA YLAPGGKQMM IDGRAGAARL RIIDGGDRMN YKPCVDVTFG SAAKVYGDKV
LSMVLTGMGA DGREGARMLK SAGSTIWAQD EESCVVYGMP QAVAKAGISS EDLPLDRIAE
RMLVEVGLA
