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Database: UniProt
Entry: A0A2Z2NKI7_9GAMM
LinkDB: A0A2Z2NKI7_9GAMM
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ID   A0A2Z2NKI7_9GAMM        Unreviewed;       390 AA.
AC   A0A2Z2NKI7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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 {ECO:0000256|HAMAP-Rule:MF_00099,
GN   ECO:0000313|EMBL:ASJ70398.1};
GN   ORFNames=IMCC3135_01395 {ECO:0000313|EMBL:ASJ70398.1};
OS   Granulosicoccus antarcticus IMCC3135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Granulosicoccaceae; Granulosicoccus.
OX   NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ70398.1, ECO:0000313|Proteomes:UP000250079};
RN   [1] {ECO:0000313|EMBL:ASJ70398.1, ECO:0000313|Proteomes:UP000250079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ70398.1,
RC   ECO:0000313|Proteomes:UP000250079};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; CP018632; ASJ70398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2NKI7; -.
DR   KEGG; gai:IMCC3135_01395; -.
DR   OrthoDB; 9793421at2; -.
DR   Proteomes; UP000250079; 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:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00099};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00099};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00099, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000250079}.
FT   DOMAIN          5..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          158..359
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   REGION          369..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        205
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00099,
FT                   ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        301
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   390 AA;  41784 MW;  9469BFB70F100133 CRC64;
     MQTKRVLVVD DSSMYQRLLS DVINTHPELE VVGVATNGKQ ALQLVESLRP DVVTLDILMP
     EMDGIQALLE LRRQWPEVRT IMVSSLTSEG SDAALDALTL GAHEYAMKPD STGGVSSIRS
     MLSDDLLPKI EALCGLASNS IKPQATQSEM YTAPNSMPLP VNLKRSADHL ELVVIGVSTG
     GPDALTKLLL QLPADFEVPV CIVQHMPAEF TGKLAARLNS ASKVSVREAQ AGDRLEPGTV
     YIAPGDFHMV LERVGLYDFV RLNKNPLENS CRPSVDPLFR SAAAIHGARC LGVVLTGMGQ
     DGFKGSEVLY TAGATIIVQD EASSVVWGMP RLIAQAGLAE AQVPLDRMAT AILDRVRAPG
     RKFVPRATAL SDDSSDVEAN GQRGLRGHGS
//
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