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Database: UniProt
Entry: A9FIU2_SORC5
LinkDB: A9FIU2_SORC5
Original site: A9FIU2_SORC5 
ID   A9FIU2_SORC5            Unreviewed;      1031 AA.
AC   A9FIU2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   OrderedLocusNames=sce1730 {ECO:0000313|EMBL:CAN91888.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN91888.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN91888.1, ECO:0000313|Proteomes:UP000002139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
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};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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DR   EMBL; AM746676; CAN91888.1; -; Genomic_DNA.
DR   RefSeq; WP_012234365.1; NC_010162.1.
DR   AlphaFoldDB; A9FIU2; -.
DR   STRING; 448385.sce1730; -.
DR   KEGG; scl:sce1730; -.
DR   eggNOG; COG1352; Bacteria.
DR   eggNOG; COG2201; Bacteria.
DR   HOGENOM; CLU_000892_0_1_7; -.
DR   OrthoDB; 9786165at2; -.
DR   BioCyc; SCEL448385:SCE_RS08905-MONOMER; -.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PF13596; PAS_10; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          59..234
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          256..519
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          706..771
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1017..1031
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1031 AA;  111610 MW;  734E6335FF5570D2 CRC64;
     MPEQKKSRRT QLGAPGPSDA APQAGRASAP GRTPVPPEDA GESAAAGGPR AEGELRFPVV
     CVVASAGGRG AIAELLRRLP SRDTSLSLVL IYSADPGELP LLELVAQSSP LPVAELRSGM
     KLAPGRVQVL PPEAQATLAG LRVELAPRGE GSPGPGDLFL RSLAGELGSG AVAVVLSGAG
     SDGALGLKDV KAEGGVTFAE NPRGAERPAL PRSAIAAGGV DFVLSVEEIA AELVRMGRPG
     HVLAPWLRQG APLGMDADLS KLLRLLHAAV GVDFSQYKKS TLRRRIQRRM TLHRLATLQD
     YLDHLRAHPG EIEDLYQDLL IKVTTFFRDP GAFAALKTHV FPVLMHSRPQ DSPVRIWVPG
     CSTGEEVYSL AISLLEFLEA DATDHAIQIF GTDLSEAAIQ QARSGIYIES ISMDVSPSRL
     RRFFVRVQGG FQVNKSVRDL CIFSRHNAAA DPPLLKLDLT SCRNLMIYLE PSLQRRLLQT
     FHQALKPTGF LLLGSSESLT TAPDLFGVVD RTHRIFCKRA ASEAAHPLAL TAPALPGAPV
     VALAPERPRE PEGFGMDAVR KEADAIVMAR YAPAGVVVDE EMQIVQFRGK TGPYLEPSPG
     DASLHLFKMA REGLVLGIRA AIDASMNSGA MARKEQLKVR QDEKIRYVDV EVWPLKVRLP
     QGRCFLVTFS ESGAARPDRP GSDPAPSDAQ KDLEIVQLRR ELVTTREYLQ SLIDELEATN
     EELLCTNDEI LASNDELHRV NDALEGAHDE LESANQELTT VNEELRSSNV ALGLANDELR
     KLLGGMNIPL LMVDADLRIR RIAGAADKLL GLAASDVGRS ILEVKSRSVA DIAPVVAEVL
     GTMSTVERRV EDRDGRSYLM RARPSRTTDD EVDGAVICWL ESEAPRRAAR ELAGARDGLS
     AVFEVLRHPF LLLDGELRIR AVTRRYCEQF MVPLGDIEGR SLSAIDAGWN TPQLEQQLRD
     VLHRRAALVD FRLEAVLAHA GRRTLSFSAF RLQADEGELP ALLLVVEDRT APEIDPAGPP
     GLRPARRAGP G
//
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