ID G2IGV2_9CLOT Unreviewed; 344 AA.
AC G2IGV2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN Name=cheB {ECO:0000313|EMBL:BAK81030.1};
GN ORFNames=RATSFB_0468 {ECO:0000313|EMBL:BAK81030.1};
OS Candidatus Arthromitus sp. SFB-rat-Yit.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1041504 {ECO:0000313|EMBL:BAK81030.1, ECO:0000313|Proteomes:UP000001273};
RN [1] {ECO:0000313|EMBL:BAK81030.1, ECO:0000313|Proteomes:UP000001273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-rat-Yit {ECO:0000313|EMBL:BAK81030.1};
RX PubMed=21925114;
RA Prakash T., Oshima K., Morita H., Fukuda S., Imaoka A., Kumar N.,
RA Sharma V.K., Kim S.-W., Takahashi M., Saitou N., Taylor T.D., Ohno H.,
RA Umesaki Y., Hattori M.;
RT "Complete genome sequences of rat and mouse segmented filamentous bacteria,
RT a potent inducer of th17 cell differentiation.";
RL Cell Host Microbe 10:273-284(2011).
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};
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DR EMBL; AP012210; BAK81030.1; -; Genomic_DNA.
DR RefSeq; WP_014094493.1; NC_016012.1.
DR AlphaFoldDB; G2IGV2; -.
DR STRING; 1041504.RATSFB_0468; -.
DR KEGG; asb:RATSFB_0468; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_000445_51_0_9; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000001273; Chromosome.
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:SF3; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 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}.
FT DOMAIN 154..333
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 344 AA; 38620 MW; 0BA9542A05FC7CD2 CRC64;
MGKTNKNLKY RDRIIKTKLI IYDESNLMKK LVYDRFSKDP SIDIIDIFHD CDEMKNFIIN
SGIVLDVIIL NQVYHDKNDF IKRLLELKNF TVNLIVISHF DSSTIEFIKQ TIGADKLIFI
KALNKSELKN IFEIKEKLVD IVYGIKNSRI KRAIFDSHKA IVIASSTGGP KVLEYIFGNL
ETKIDMPVFI VQHMPEGHTK QFADRLAGLC SYKVCEGKNG EIAIANVIYI APSGYHMELD
CNKQIKLNVN KPINNVRPSA DILFCSASKI YKKGLLGIVL TGMGKDGSDG IRNVKINGGI
TIAQDEGSST VFGMPKSAIE TGMIDKILSK DEILFEIVKH SGKL
//
