ID E0USU0_SULAO Unreviewed; 1441 AA.
AC E0USU0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN OrderedLocusNames=Saut_0068 {ECO:0000313|EMBL:ADN08117.1};
OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS OK10).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08117.1, ECO:0000313|Proteomes:UP000007803};
RN [1] {ECO:0000313|EMBL:ADN08117.1, ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX PubMed=21304749;
RA Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10).";
RL Stand. Genomic Sci. 3:194-202(2010).
RN [2] {ECO:0000313|Proteomes:UP000007803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC {ECO:0000313|Proteomes:UP000007803};
RX DOI=10.4056/sigs.1173118;
RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Sulfurimonas autotrophica type strain
RT (OK10T).";
RL Stand. Genomic Sci. 3:194-202(2010).
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; CP002205; ADN08117.1; -; Genomic_DNA.
DR RefSeq; WP_013325873.1; NC_014506.1.
DR STRING; 563040.Saut_0068; -.
DR KEGG; sua:Saut_0068; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000892_2_1_7; -.
DR OrthoDB; 9786165at2; -.
DR Proteomes; UP000007803; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; IPR013767; PAS_fold.
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; 4.
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; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 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; 4.
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; 4.
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:ADN08117.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000007803};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..190
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 182..453
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 695..752
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 825..896
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 901..953
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 954..1024
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1028..1080
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1081..1123
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1222..1437
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 622..695
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1441 AA; 165186 MW; 8500FC19B716C5FF CRC64;
MKDSVFIGIG ASAGGLEALK ELLPLLPQDE GYVYIIAQHL DPHKKSALGE ILTAYTAMPV
VTISQKYTFL PNSVNIVPPG YNLTYAKHKL LLEKISKTPH TPTPSVDELF KALSSYKKEN
CVGIVLSGAG HDATAGVKTI KENGGITVAQ SPDEAQYADM PKNAIQSGYI DYVLKVAQIG
ENLESIIHIM PEPLMKITKL LEEKECLDID KYKKETIMRR LNKRMMLTKC ADLDEYFDYI
QTHPDELYLL YQNILIGVTE FFRDKESFEV FKQHLEHYLL DKPDHYDLRI WSIACSTGEE
AYSLAIIIDQ IKKKLKKNFS VHIFATDIDE KALEIAKKGI YTKKLLEKID KKIIKTYFSA
LDEGYKIKEF IRSQIVFTKH NILSDPPFIK QDIISCRNFL IYILPEVQQE LFVLFHYALK
DKGLLFLGSS ESTLMSVDYF KALNQEHKVY VKEALQNPPR ISSHYFSSHI NTKQNQTGIK
TSTLKDINIK EEITNTVFEL FSHECIIVDT NFTIVYKQGS NPFLELGDGF VTLNIVENLK
KELRYSVKKI LKRTLKTATL HSTKFIEVKL DNKEQTFVKV IAAPFANKQN TPFILLYFQE
LNAHGLEFDT REIVLPNESY VVENLTNRVK ELQEDYHALL DELSISKENM QLLNEELQRS
NEELQSANEE LETSNEELQS SNEELQVSII NEQKLQRQLA LILNSTHDGI MGLDLEGRHT
FVNAAALEML GYTKDELLGK NAHRIWHHTK PDGSHYLFSE CTLHTHLVDG LSVRKEDFFF
KKDSTGFNVE VLQNPIIEEG KVKGAVLSFR DITEKKKLQQ EAEYEHRLAN LYVNTTGTLV
MVLDLAGSVN MINNSGCELL GLPKEKIIGK NFIHNFIPKA RQPENQNVFD SLISEKTDIL
KEYKNIIIDA QGKEHIISWR NNYIKDDNGT LTSLLSSGID ITDKEALTEK LFEQEHLYKL
TFEEADIGIA HVSLDGRWID TNEYLSKLLG YTKEEFQNMH VFDITFPQDR DTDMHMIEQL
HKGEKKSYHI EKRYVHKNGN IIWVSLAVVL LLDEQKKPLY LLKIIRDISQ LKLLMYQIEI
EKNRFQRIIE FTPIPTMLYN TDGDILILNK IFQDNTGYTL EEIPTIDKMV EKLFVNEDAD
SIKSIKQYYK EPTKLPKQQQ CITTKSKERR VGILDAVKLD EEGNSSEILY LIAIVDITDI
QKKDELMVAQ SRQAAMGDML SMIAHQWRQP LSVISMVANN IQAQIELQRS VDAKSLHDLI
HTLNEQTQYL SHTIDDFRNF FKPDKNREFI KIDVILEKLT HLIEKSLQNN AISLTLPKKS
DIELCTYQNQ LLQVLINIIN NAKDAIKEHR AQDGNISIDV IKKKKEILLK ICDNGGGIKP
EILKKLGEPY VTSKSKNGTG LGIYMSRIIV EKHLGGRLSW ESNSKGSCFY ISLPKDTICE
S
//
