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Database: UniProt
Entry: H1Y664_9SPHI
LinkDB: H1Y664_9SPHI
Original site: H1Y664_9SPHI 
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
//
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