ID H1Y664_9SPHI Unreviewed; 1176 AA.
AC H1Y664;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=Mucpa_6976 {ECO:0000313|EMBL:EHQ31023.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ31023.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ31023.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ31023.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) 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; CM001403; EHQ31023.1; -; Genomic_DNA.
DR RefSeq; WP_008513165.1; NZ_CM001403.1.
DR AlphaFoldDB; H1Y664; -.
DR STRING; 714943.Mucpa_6976; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000892_0_2_10; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000002774; 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 CDD; cd00130; PAS; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 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); 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.
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 Kinase {ECO:0000313|EMBL:EHQ31023.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..191
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 200..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 962..1176
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 636..709
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 15
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1176 AA; 131462 MW; 4ED326E60F18AD79 CRC64;
MQLTAPHHII AIGASAGGME EINVFFDHTP LDGVSYIIIQ HLSSDFKSRM VDLLARHSKL
IVKEAAQGMK VMSNEVYLIP NDKYMTISGE ELFLSDKKDI KGPHLTINTF FTSLATDCGK
KAIGIILSGL GSDGTEGIKA IKKAGGIVMA RNPETSGFPS MPAHVIATGL TDFILEPALM
PAAIEDYIKY GLEISEEDDD KNIKSIVDLI KANSPLDFSD YKQATILRRT RRRAAAANFP
SLSNYLAYLK KNPDEVEVLS KDFLISVTSF FRDKQAFEVI QKEIIPALLQ LLAPDEELKI
WVAGCATGEE VYSLGILIQE QLQGNFKDTV VKIFATDVDN LALAHAGRGL YSLSIKKHVS
TERLEKYFIN EGSAFRISPA IRKMVIFAQH DLVKNPPYCN MHFISCRNLL IYMTPVLQKK
VFAMLLFGLK KDGYLFLGPS ENPMHIIKNL RVVSSKWKIY QNLVAKRTVN FDAFSMPDYL
DTKHSLPMPM AETMSKDARQ TIVETVVTGL TEDLDFLSLC VDEKNQVVKS FGDTKKYLLQ
KHFTTNLAEL LSKPLAVAFS SLSKSVLNTG KKAVVEHIKM KIGRRTLKVN MAVRPFPADQ
SNRKMLVVTL NEDKSGSVAE NKVDVYDPKV YQDQYAINLE EEVKELKDKL QSALEKLDSS
NENMQSFNEE LISANEEMQS TNEEMQSVNE ELHTINAEYQ SKNKELLETN DDMNNYFRSN
VNGQLFVDDD LLLMKFSPGA VKQINLLPSD IGRPLSNIST NIKFETILAD ITEVLAKGNV
ITKEIETNNG DWYQVMTMPY VRQADNKRNG AIITFNDISE LKKAQQELDL SSKMLGMAIE
AAELGTWSIN VKTREFTSSS RLKELFGFES AQMMTFPAAI AQIAGNYQLI VSEAIEETIN
GGKKCDIEFP SQGHHDGKLR WIRAVGNLTH NKENIPNYFS GVLLDITVHK LNELRKNDFI
AMVSHELRSP LTSLQANMQL LALKAKKNDD EGTLLAVEKA NKQIKKMGTM ITGFLDAASL
EEGKIYLRTQ TFEVNGLLQE IKEEMLTTTT NHQINLLPFK TISVNADRNK IGQVVTNLLS
NAVKYSPKGG NIEVSCRTVR SIVEVSVTDE GLGISLPDQA KLFDRYYRIE SASNAKIAGF
GLGLYLSNEI INRHKGRLWV DSELGKGSTF HFSLPL
//