ID A0A3B7MFA7_9BACT Unreviewed; 1261 AA.
AC A0A3B7MFA7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=D3H65_03090 {ECO:0000313|EMBL:AXY73014.1};
OS Paraflavitalea soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Paraflavitalea.
OX NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY73014.1, ECO:0000313|Proteomes:UP000263900};
RN [1] {ECO:0000313|EMBL:AXY73014.1, ECO:0000313|Proteomes:UP000263900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY73014.1,
RC ECO:0000313|Proteomes:UP000263900};
RA Weon H.-Y., Heo J., Kwon S.-W.;
RT "Genome sequencing of strain 6GH32-13.";
RL Submitted (SEP-2018) 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};
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DR EMBL; CP032157; AXY73014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7MFA7; -.
DR KEGG; pseg:D3H65_03090; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000263900; Chromosome.
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; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
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 PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 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; 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); 1.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..206
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 232..496
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1030..1255
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 674..739
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 986..1020
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1261 AA; 142612 MW; C38E4DEA3518DE2E CRC64;
MKSQSPTYQK TLGKGIIEEP DYIIAIGASA GGLEAIHEFF DNMTEVGNYA FVVIQHLSPD
YKSLLVELVS KHTRMKVLEA EHNVVLQKRC VYIIPNNKVM TIRQGKVQLV QKALNKAPNT
AVDTFLYSLA QDKGPHAIAV ILSGTGSDGT RGVEAIKKAG GIVLVQSPES ARFDGMPNSA
INGGSVDHVL SPADMPAAIV KHIMAHRAAA NGNGNENENG NGNGHTSPPT QEELLQEITH
LIKLNTGNDF HAYKPATILR RIEKRMMKLE LHTLEEYVAY LHQYPDESNT LYKSFLIGVT
RFFRDKQAYE VIRTQVLPAL VKTKQPGELL KVWVNACSTG EEAYSLAIIF ESYLRKHDLQ
LDVKIFATDL DESAIEYAAR GVYPLSIEKD IDKDILEAYF IREGKKYMIT PSIRKAVVFA
RHNVLKDPPF IHNDLVSCRN MLIYMDNSLQ QKVLDTLDFS LRVGGFLFLG SSEHLSGLKE
NYVETEGKWK IFRKVNLKRR HYIEPVYNTG RSYRQVQTTR TEPLLLSNKK QEEHSLVEAF
KDLMADEAKY AALYIDSRYE VKDAIGEFTR YLALPERKLN FHLLKMLLPE LSVPINISIR
KAWKDKKKVT VRAIRVKRAD QTVLVNAIIH PYPPDKNPCT LVVMWETPDT SGDELEVKRH
HLSPDSQALI LELEDELQES RSNLQIAVEG LETANEELQS SNEELLSANE ELQSSNEELQ
SLNEELHTLN TEHQLKIREL IELNDDLNNY FGSTDIGQVF IDGEMRIRKF NPAAIKLINL
IDSDIGRPID HISNNIEHST LLEDIKHVLR SKKLVEREVK LINRTSALMR IFPYIRSDKK
TDGAVITFID ISMIKNLDNI ITGIFNSTLN AIIAFKAQRS ASNEIADFHV LTANKAADAL
LAANSEKAAG FSMKYDFQHL CSNGIFQKLV KVVEDNKAFH DECTVTIGET SVTYEMIAVK
MMDGIIITYS DITEKKEAER QLHKSYSELL IAKDALKQLN LELEEKVAEG IRANKELEKS
NTELQQYAFV ASHDLKEPTR KIFIFSNMIK DNYLKDTESK ATDLVNRIIK SSQRMMRLIE
DLLNYSRLSQ NGVFEPVDLT ITIREILSDL EVVIDDKKAV VKLENLCKID GMPGQLRQVF
QNLISNALKF SRKDIAPEVH IRAQRVAART FDAPEDAEGA YCRIEVSDNG IGFHERFLDK
IFTLFQRLHT QEQFEGTGIG LAITRKIIEK HGGIITARST EGVGTTFIIV LPMHQTTVRP
V
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