ID W6TIV8_9SPIR Unreviewed; 383 AA.
AC W6TIV8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=BDCR2A_00688 {ECO:0000313|EMBL:ETZ18715.1};
OS Borrelia duttonii CR2A.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=1432657 {ECO:0000313|EMBL:ETZ18715.1, ECO:0000313|Proteomes:UP000019148};
RN [1] {ECO:0000313|EMBL:ETZ18715.1, ECO:0000313|Proteomes:UP000019148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR2A {ECO:0000313|EMBL:ETZ18715.1,
RC ECO:0000313|Proteomes:UP000019148};
RA Schwan T.G., Raffel S.J., Porcella S.F.;
RT "Comparative genomics of relapsing fever spirochetes.";
RL Submitted (DEC-2013) 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:ETZ18715.1}.
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DR EMBL; AZIT01000001; ETZ18715.1; -; Genomic_DNA.
DR RefSeq; WP_038366430.1; NZ_AZIT01000001.1.
DR AlphaFoldDB; W6TIV8; -.
DR PATRIC; fig|1432657.3.peg.679; -.
DR Proteomes; UP000019148; 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:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16432; CheB_Rec; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR008248; CheB-like.
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 PIRSF; PIRSF000876; RR_chemtxs_CheB; 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:UP000019148}.
FT DOMAIN 194..383
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 383 AA; 42543 MW; 8140B5C383054573 CRC64;
MKILVIDIQG LIRQVFVRAF SKDVDVEILN PGSNSLNLIN VFLQKFPDVV IIDENTAKSH
FGNSLNNVLN NISLPVVFIA ENEVYPKFGF LDSKKDKIKL IINKLNFKLT VNLFRSDYLD
LIKSEIKKLV DHKFVASFES KRIKSPDFFE KTESKESERD ITNITKSYKV ADVINVSPKN
GPDVILKYQG VINKNKTGKV IFVGASTGGT EALRVFLKLF KKDSPPIVIV QHMPGGFTTS
FAKSLNNEFE VDIKEAEDGD ILRPGLVIIA NGHYHLIVKY ANGNYFTHLI DGPPVSRHKP
SVNVLFRSAA MYAGENAIGV MLTGMGDDGA SCMLEMKNNG AYNIAQDQLT SVVFGMPMEA
IKIGAVDKVL PLNKISECIL RRS
//
