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Entry: A0A0H4W5E6_9BORD
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ID   A0A0H4W5E6_9BORD        Unreviewed;       349 AA.
AC   A0A0H4W5E6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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_1 {ECO:0000313|EMBL:AKQ56011.1};
GN   Synonyms=cheB {ECO:0000256|HAMAP-Rule:MF_00099};
GN   ORFNames=ACR54_02696 {ECO:0000313|EMBL:AKQ56011.1}, CS347_17425
GN   {ECO:0000313|EMBL:AZW18416.1};
OS   Bordetella hinzii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ56011.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|EMBL:AKQ56011.1, ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|EMBL:AKQ56011.1,
RC   ECO:0000313|Proteomes:UP000036382};
RX   PubMed=26316634;
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT   Humans.";
RL   Genome Announc. 3:e00965-e00915(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA   Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000282741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA   Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA   Williams M.M.;
RT   "Whole genome sequencing of various Bordetella species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AZW18416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H720 {ECO:0000313|EMBL:AZW18416.1};
RX   PubMed=31744907;
RA   Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA   Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA   Unoarumhi Y., Williams M.M., Tondella M.L.;
RT   "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT   Bordetella Respiratory Pathogens.";
RL   mSystems 4:e00702-19(2019).
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; CP012076; AKQ56011.1; -; Genomic_DNA.
DR   EMBL; CP024172; AZW18416.1; -; Genomic_DNA.
DR   RefSeq; WP_029577896.1; NZ_LT906461.1.
DR   STRING; 103855.ACR54_02696; -.
DR   GeneID; 56621943; -.
DR   KEGG; bhz:ACR54_02696; -.
DR   PATRIC; fig|103855.14.peg.2659; -.
DR   eggNOG; COG2201; Bacteria.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000036382; Chromosome.
DR   Proteomes; UP000282741; 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:SF6; PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE; 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|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW   Rule:MF_00099};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00099};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_00099}.
FT   DOMAIN          5..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          151..339
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   349 AA;  37601 MW;  2361E11E837FE8C4 CRC64;
     MKKIKVLCVD DSALVRGLMT EIINSHPDME VVATAPDPLV ARELIKQHNP DVLTLDVEMP
     RMDGLDFLEK LMRLRPMPVV MVSSLTERGG EITMRALELG AIDFVTKPKL GIRDGLLEYS
     ELIAEKIRAA SRARLRAPAP ASATPLRLRS PYTSSEKLVI LGASTGGTEA IREVLQPLPP
     DSPAILITQH MPAGFTRSFA QRLDALCAVT VREASHGERV LPGHVYLAPG GEQHMKLGRS
     GANYVIELQA SEPVNRHRPS VDVLFQSAAQ AAGRNAIGVL LTGMGKDGAA GLLAMKRAGA
     HTLAQDEASC VVFGMPREAI QLGAADEVVP LSEMSERILM RAGDRGHRV
//
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