ID A0A252D3C2_9NOSO Unreviewed; 372 AA.
AC A0A252D3C2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=BV372_31065 {ECO:0000313|EMBL:OUL21969.1};
OS Nostoc sp. T09.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL21969.1, ECO:0000313|Proteomes:UP000195076};
RN [1] {ECO:0000313|EMBL:OUL21969.1, ECO:0000313|Proteomes:UP000195076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T09 {ECO:0000313|EMBL:OUL21969.1};
RA Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA Cibrian-Jaramillo A.;
RT "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT cycad coralloid root endophytic microbiome.";
RL Submitted (JAN-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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:OUL21969.1}.
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DR EMBL; MTAV01000199; OUL21969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252D3C2; -.
DR OrthoDB; 480201at2; -.
DR Proteomes; UP000195076; 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:InterPro.
DR CDD; cd16432; CheB_Rec; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 Pfam; PF13185; GAF_2; 1.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR PROSITE; PS50122; CHEB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000195076}.
FT DOMAIN 8..198
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
SQ SEQUENCE 372 AA; 39924 MW; 5CFE0D5CE72889FE CRC64;
MPRQRSNNKS NIEIVAIAAS AGGVTAIRKV LSGLPADFPA PILCLQHLNP SETNVLAQVL
QLQTNLTVRW AHEREELTAG VVYVCPPGHY FVVHANGTVS LAPQATKHGW VHGVNHFFES
VAQSYADRAV VVVMTGTGKG GAEGVRAVSQ QNGIVLAQDK ASSVAYGMPE AAIATGCVDR
VLPREAIASL LVSLVCEGNP LSNELVSKTS SLLIAGLPIS PTFQDALENV LDRAIAIHRT
DMGYIHLLDR QTCTLALAVQ RGFDVGLVDE LQTVSITEYS PCIMALRAGE TVIVEDVKVD
PRFTPHRAIA AAAGYRAAQS TPLASRTGTL LGVLSTHFRQ PRKFVPWEMK LLDMHARYAG
DLIELFQAKK VG
//
