ID A0A0P4UPS8_9CYAN Unreviewed; 346 AA.
AC A0A0P4UPS8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein-glutamate methylesterase {ECO:0000256|ARBA:ARBA00039140};
DE EC=3.1.1.61 {ECO:0000256|ARBA:ARBA00039140};
GN ORFNames=NIES2104_06450 {ECO:0000313|EMBL:GAP94135.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP94135.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP94135.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP94135.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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:GAP94135.1}.
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DR EMBL; BBWW01000001; GAP94135.1; -; Genomic_DNA.
DR RefSeq; WP_058995592.1; NZ_BBWW01000001.1.
DR AlphaFoldDB; A0A0P4UPS8; -.
DR STRING; 1552121.NIES2104_06450; -.
DR InParanoid; A0A0P4UPS8; -.
DR OrthoDB; 9793421at2; -.
DR Proteomes; UP000052243; 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; cd16433; CheB; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR011247; Chemotax_prot-Glu_Me-esterase.
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; PIRSF036461; Chmtx_methlestr; 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 1..178
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 346 AA; 37838 MW; 9C3AB984B07E3154 CRC64;
MPGHDIIVIG TSAGGLKALG AIVGALPADL DAVLLVVQHL EPNKPSILPK ILSDVGSLPA
SHPVDGEAIQ SGRIYIAPPD YHLLLNQGYV RVVRGPQENR FRPAIDTLFR SAARAYGPRV
LGVVLTGYLD DGTVGLQAVK KRGGVAIVQD PKEAEYPSMA KSALQFVKVD HCLPLADIPN
LLVRLSKEPA ESEEAYPVTQ EIEVESNIAE QKMNTQEFLK NVEAIGTRTT YTCPECNGSI
WQIGNSEPLR FRCHTGHSFT ANVFLAEQTQ NLENALWSAI RVMEEKVTFS RQMAERMEGH
SLLDAATKYN DHANRLDEEV ALIRGIVLNG FATKRTIAED EEEQPA
//
