ID A0A1V6LRI9_9FLAO Unreviewed; 1480 AA.
AC A0A1V6LRI9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=BUL40_09370 {ECO:0000313|EMBL:OQD42719.1};
OS Croceivirga radicis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceivirga.
OX NCBI_TaxID=1929488 {ECO:0000313|EMBL:OQD42719.1, ECO:0000313|Proteomes:UP000191680};
RN [1] {ECO:0000313|EMBL:OQD42719.1, ECO:0000313|Proteomes:UP000191680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSG9 {ECO:0000313|EMBL:OQD42719.1,
RC ECO:0000313|Proteomes:UP000191680};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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:OQD42719.1}.
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DR EMBL; MTBC01000005; OQD42719.1; -; Genomic_DNA.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000191680; 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:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; PF08447; PAS_3; 2.
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; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
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; 3.
DR PROSITE; PS50112; PAS; 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|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000191680};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..193
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 208..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 791..841
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 919..971
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 994..1046
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1049..1102
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1120..1341
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1365..1480
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 638..728
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1415
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1480 AA; 169060 MW; 424E9D95DAC7FBC6 CRC64;
MGSKQDGFMV VAIGASAGGL QAIHTFFDAM PASPDMAFIV VQHLAPNFKS LMPELLASHT
KMKIFVAEEN QEIKPNCIYL NNKDNNLGIE DGKFTLLKKA PRKQLNLPID IIFKMVANAY
KENAVGVVLS GTGSDGSKGI YNLKEVGATI YAQDPKSAEF DGMPKSAIHT NCVDFILPPQ
KIAENILWLA NQERDFQTLI NPQNATVYDT IITKLYKHSG IDFSKYKPNT LIRRMNKRMS
LLQLNSLDVY YQYLLTNEEE LKLLSQSFLI GVTSFFRNVE AFNSLKLSVI PELFANRLPE
ETIRIWIPGC SIGKEVYSLA ILLDDYLQSQ ESNLNFKIFA TDIDRYALKK AGNAVFGIND
ISEIGEEYLT KYFIKKGDRF QIIKRIREKI IFSYHDLTND PPFIQIDLIS CRNLLIYLNK
ETKEKVINAF EFSLNKNGFL FLGNSESLAK AEQNFTVVNG KHKIYRIKKG RNLLENNALQ
IKNKTHSKIN YLNLTNKVEQ NHNYTARKEV LFYKHLSKKH APVTVYVNQD YDVIFMLGDF
QKWFSQNDGI FNNNLLNLVN PELASIIRNG IRRAKTSDKT ISYKKLSCAV PSGQILTDLF
VERVQLEPNG DFLYMLQFGE SIGQENTEEV VLSNEDISTL AQQQIDDLEY ELSEKKEALT
NITEELETSN EELQSSNEEL MSSNEELQSS NEELQSVNEE LYTVNTEFQE KNKELEELNN
DMNNLLDSTD IGTLFLDEAL KIRKFTPALK KVFKLESQDI GRPIFNFSSV FEEEARLRIL
NKSKDALTTF NTFEEQLLDS TGNWYLIRIS PFVTKEKRIS GVVITFVDIT EIKKAEEELK
LKTRELTIAQ EVAKLGSWTL NIATNEVYWS EELFKMYGLD PEDGVPDYDD ENHRKLFTPK
SWATLEKAVS TTIETGKPYT LELRSIRNDG SKGWMYAVGR VLKNEEGKPT HLQGIAQDIT
ERKQLRSKLQ KADEFAGKMT RLSPSGMYIY DMVKGSNVFM NEGYTNILGY TPADIEKLSP
DEFFNLFHPD DQHLIEKHMA KVLEGKLENI VEYRFKHKNG KWVWCYSIDS PFEKDDEGKV
TSFFGVFIDV TQKKENEEKL KKALVEANSA NIYKNQFLAN MSHEIRTPLN GLVGFSNLLR
DHDLNVNDKK EYISIIENCS QQLLSLVDDI IDLSKIEAGE LDMEFMPCEL NHLVRELEMT
FNEIKKQQEK DNLEIKTFVP NPNVPLNIKT DPNRLKQVLI NLVNNAIKFT DSGSVTFGYA
IKGDWVEFKI KDTGIGIAEE NLKLIFERFE RIGFENNDKY SGKGLGLSIS KGIIGLLGGD
IDVSSKLGVG SEFTFTIPFT LVETVKPMEN KSSAKQINKL FNDQKILVAD DNRINRHYLK
TLLKRTNLLV DYAENGEEAV SMFRQKPDYD IVLMDIRMPV MDGFEAKEEI VKINPNAKVI
AQTAHAMSND REQCLSRGFV DYIAKPLGKE DLFEVIAKWI
//
