ID A0A261GUN7_9GAMM Unreviewed; 349 AA.
AC A0A261GUN7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=BTA51_01855 {ECO:0000313|EMBL:OZG75154.1};
OS Hahella sp. CCB-MM4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=1926491 {ECO:0000313|EMBL:OZG75154.1, ECO:0000313|Proteomes:UP000215632};
RN [1] {ECO:0000313|EMBL:OZG75154.1, ECO:0000313|Proteomes:UP000215632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM4 {ECO:0000313|EMBL:OZG75154.1,
RC ECO:0000313|Proteomes:UP000215632};
RA Sam K.-K., Lau N.-S., Dinesh B., Go F., Amirul A.-A.A.;
RT "Genome sequence of Hahella sp. CCB-MM4 and discovery of its potential
RT applications.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG75154.1}.
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DR EMBL; MRYI01000001; OZG75154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261GUN7; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000215632; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
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 SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Reference proteome {ECO:0000313|Proteomes:UP000215632}.
FT DOMAIN 145..339
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 349 AA; 38036 MW; 5C1249506C725FD7 CRC64;
MPDQQAVIGL ISDCPLQRHI MQAAIEGYGF AVAANSDPAR IDKEFLERYM LVQAWVVILA
DEDLWSEAID ALIELSEAPI LFGLGEAPGK HSPEYAKWER RLYSKLVELV GEPETLSEHV
ETLNDLDSLI NRNPQAIPLP HHIRPATASD PVERVVILGA SLGGPAAVKG FLDCLPVGLP
AAYVYAQHID QNSANVLVRV LGRHATVKLS EAHHGNSLHN GEVVIMPVDQ EVTFDEDGAM
FFQEHEWPGP YGPSIDQVML NVANYYGSKV HAILFSGMGN DGAIAGPLLK AYGSRIWTQT
SESCANSSMP DSVADTGCVE FRGTPVQLAD KLVKTIELEE LSKRRRGIG
//
