ID A0A367R899_9NOSO Unreviewed; 1405 AA.
AC A0A367R899;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=A6770_19970 {ECO:0000313|EMBL:RCJ31652.1};
OS Nostoc minutum NIES-26.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ31652.1, ECO:0000313|Proteomes:UP000252107};
RN [1] {ECO:0000313|Proteomes:UP000252107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tabuchi Yagui T.R.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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:RCJ31652.1}.
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DR EMBL; LXQD01000225; RCJ31652.1; -; Genomic_DNA.
DR Proteomes; UP000252107; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000252107};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..208
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 224..496
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 822..875
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1027..1245
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1279..1399
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..751
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1330
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1405 AA; 156318 MW; 0B63F4B0454A1DD3 CRC64;
MTSRRSSKKS QSNSTPAKTS DAEQEENQLF PIVGMGASAG GLEAFAELLS HLPTDTGMAF
VLVQHLSPNQ KSLLSEILSR TTQMPVTEVE NGMSVEPNHV YVIPPNTTMT ISQGVLKLIP
REKVFGLSKT VDAFFISLAQ ERGSKAIGVV LSGGDADGTR GVEEIKGAGG ITFAQSEKSA
KVNSMPNTAV ASGHVDFILT PEAIAEELAK ISRHPYVSHR SVSKLTEPLP EGEDVLLVIF
NLLRTAKGVD FNHYKQTTLK RRILRRMILY KLERLEDYLR YLQDNPAEVS ALYQDVLIAV
TSFFRDPEAF EALKSKVFPV IAKDRTPESP IRIWVSGCST GEEAYSIAIC LLEYLTDSGI
NPPIQIFATD INEVAIEKAR IGIYKPSEVA DVSPERLQRF FIQVESGYQI GKPVRELCVF
ARQNLIADPP FSKLDLITCR NVLIYLGAAV QKKLLPIFHY GLKLTGFLML GTSETVGEFS
DLFSLVDRKY KIYARKVAST QLGIALPMSN HPVETANPQP PVSEDDWNDL EMQKAADKIV
LSKYAPAGVI VNNNLVILQF RGQTAPYLQP SPGRASFNLL KMAKEDLRLE LRTAIHQAKK
REIPVRKEGL QIRENDRVRQ VKIDVIPFKP IAAAESYFLV LFEDTSPSLP PASEIAGDRN
LSARRRNPTA DQQEIIQLKQ ELATTKEYLQ SIIEEQQATN QDLRAANEEI LSSNEELQST
NEELETAKEE IQATNEELNT INDELQRRNL ETTQVSNDLQ NLLSSINIPI LMLGGDLRIR
RFTPLAALIF NLISTDVGRP LSDINHNLNL PDLEQQILEV INTLNLKTQE VRDQDGYWYD
LRIRPYRTID NKIDGAVVVL VDINALKRSA EQVRASRDYA EAIVDTVRES LVVLNLDLRV
ITANQSFYET FQVTPTETEQ RLIFEIGNGQ WNIPQLRSLL EDILQNNAQF QDLEVEHNFE
QIGQKTMRLN GRKMPQTDDI PMILLVIEDI TRRKQLEAER TQLLTQEQSA RAAAETANRA
KDEFLSIVSH ELRNPLNSLL GWANLLRKQQ LDEARTKQAI ESIHRSAKAQ AQLIADLLDI
SRVSSGRFRL NVQSIELAPI IEAAIKVVSI SAETKNIQIE SRMEPATKRM LGDPIRLQQV
IWNLLSNAIK FTPVGGRIEV TLEYFDLQAQ IQVSDTGQGI NADFLPYLFE RFRQADGART
RSNPGLGLGL SIVRHLVELH GGTVDAQSQG EGQGATFTIR LPLQTNLQEI SLPSTEEAVV
SIEEPEVLLD TILSLEGVRV LIVDDETDIR ELFTTVLEAY GGEVTAVTSA SEALSTLMAN
PGGYDVLLSD IGMPEEDGFM LIGQVRMLSP ELGGRIPAAA LTAYAGDVEQ TEVLAAGFQM
HIAKPVEPDR LVFIVASLAG RIRNT
//
