ID G8TRP8_NIAKG Unreviewed; 1527 AA.
AC G8TRP8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN OrderedLocusNames=Niako_5966 {ECO:0000313|EMBL:AEW02195.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEW02195.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEW02195.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
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., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-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; CP003178; AEW02195.1; -; Genomic_DNA.
DR RefSeq; WP_014222105.1; NC_016609.1.
DR STRING; 700598.Niako_5966; -.
DR KEGG; nko:Niako_5966; -.
DR PATRIC; fig|700598.3.peg.6110; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2433; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000892_2_4_10; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000005438; 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:UniProtKB-EC.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 4.
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; 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 NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 2.
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 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); 4.
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; 2.
DR PROSITE; PS50112; PAS; 2.
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 ECO:0000313|EMBL:AEW02195.1}; Kinase {ECO:0000313|EMBL:AEW02195.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AEW02195.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEW02195.1}.
FT DOMAIN 10..200
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 216..453
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 992..1065
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1069..1121
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1129..1199
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1202..1254
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1283..1509
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 671..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 954..995
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1527 AA; 174978 MW; CFD4A03D3A562D52 CRC64;
MLFFTKNNTP QQDDTYVIGI GASAGGLEAI NELFDNVSYS ENIAFIVVQH LSSDYKSLLV
ELLGKHTHMP VEEAGHRQRV EPGKVYVIPN NKELTIHNGL LILAEKEFDK GPNTAIDTFF
QSLARDQRQF AVAVLLSGTG TDGTRGIEAV KDHGGFVIVQ NPATARFDGM PKSAIGSGYA
DLIVSPDEVF SQIENHIDGV IPSKNTSSKN YNDGVQNILS IIYRKTGYDF LQYKEPTIVR
RLTRRMQMLK LEDIQAYERY VAAHEEEPLM LTREFFIGVT NFFRDKDAFD CLNRQVILKL
VESKEEQESL KVWVTACSTG QEAYSIAILI DKAQQQFNKQ FEVKIFASDI DKSAVEFASK
GKYSYNQLLG LDKKIQQEYF TEVEDGMVII PRIRKQVVFA AHDITKDPPF IKNDLITCRN
MLIYLNPSLQ ENVLSTLHFS LNSGGYLFLG TSENPSLLRK GFTEVNNKWK IYRRTTDQNT
YARGVLNSAR NKLAALTTNT GSKTKTDVQL SDDFRNVLAD KMGFAGMYLN DNYEIKEAIG
NFRKYLTLPD KLSTLNILKM APSELSGMLS TTLRKVLKEN AKQEIRNVRV RLNEEQRMLD
VFIYPPRETS NGSYSLVVFA DSILKGDKTP VMVQDVSELQ KDQYVSQLED ELRETRTNLQ
MAIESLETAN EELQSSNEEL QSANEELQSS NEELQSLNEE LHTLNTEHQI RIKELVELND
DISNYLQTSQ IGQIFLDQKL RIRRFNNSVA SVFNIIEGDI GRPIDHITHH IKASSFAEDI
KKASKSGAVI EREIELDNGN VYLLRILPYI RQDKVRDGLV ISMVDISATR NLNTLVKSVF
EASANPIFVF ESKRGEDGKI IDYTCKIANH NAYHSLGTLM KEDRMSLTKD FPELASTQLY
KKYNEVVNTG EPALGLEINF TKNGNKQWFQ AGINKMQDGF VLVLSDITLR KEAEEKLRRN
YNELLITKET LRELNNQLEK KVRERTRDLE ESEERFRMVA SLTNDVIWDW NFAENNVWWS
DSFYELFGYG KDEKLVQKHF FRLKHIHIDD RQRVEEAINA TLENPRKEFN VGYRFQKQNG
EYAYVLDRGM LLTDDQGIPY RMIGAMVDVT RLEQSNQQLQ EKKIELQTQI GQFRFVTDFM
PQIVFSAYAD GNFDFFNQKW YDYTGLTPEQ TLNNGWMGVL HPQDLERARK TWQQSLTNGN
TFQFENRMRR TDGAYRWFLV RALPMRDEKG VIEKWFGTFT DIHDQKLAEQ LLEEKVQERT
RELRLTNEKL EASNADLMQF ASVASHDLKE PLRKIHFFSG LIKEMFAEEA STKDLEAYID
RIISASSRAT SLINDVLSYS RLSSENLVEE VDLNKIVGEI LQDLELVIGE KNARIQVGHL
PVIQAVSGQM RQLFQNIIAN SLKFHKPGQS PVIYITSKPV ENADYPEMKD AAGQLYEIRM
KDEGIGFEDQ YSRKIFSLFQ RLNSKEKYEG TGIGLAIANK IVERHHGVII ARGHKHDGAE
FIIVLPETQP VVHSDNDGQA KNELIIK
//
