ID Q7NFG3_GLOVI Unreviewed; 1225 AA.
AC Q7NFG3;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN OrderedLocusNames=glr3562 {ECO:0000313|EMBL:BAC91503.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC91503.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC91503.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC91503.1; -; Genomic_DNA.
DR RefSeq; NP_926508.1; NC_005125.1.
DR RefSeq; WP_011143551.1; NC_005125.1.
DR AlphaFoldDB; Q7NFG3; -.
DR STRING; 251221.gene:10761077; -.
DR EnsemblBacteria; BAC91503; BAC91503; BAC91503.
DR KEGG; gvi:glr3562; -.
DR PATRIC; fig|251221.4.peg.3595; -.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000892_2_2_3; -.
DR InParanoid; Q7NFG3; -.
DR OrthoDB; 9799157at2; -.
DR PhylomeDB; Q7NFG3; -.
DR Proteomes; UP000000557; 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; cd00075; HATPase; 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
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:BAC91503.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..181
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 206..481
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1005..1221
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 688..747
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1225 AA; 136679 MW; 188EF61DB589633D CRC64;
MDVGREPEQQ QPGDLDLFAV VGIGASAGGL EAFTQLLSHL PNHTGMAFVL VQHLDPSHRS
LLAELLSRTT QLPVVEVHDG MTLEADRVYV IPPNTQMTLA RGALQLAPRE KVQGRYMPID
AFFRSLAQER GSRAIGVVLS GSDGDGALGL EAIKAAGGIT FAQCEASAQF SDMPHRAAAT
GVDFILPPQA IAEELVKISA HPYVIPARSN MPADEEALPS VFALLQAATG ADFTYYKRTT
LLRRLRRRMV LHKLERLVDY VRHLQDNPGE VQTLYEEILI SVTSFFRDPD VFAALQEKVF
AGICQGKAAG SPIRVWVPGC ATGEEVYSIA ITLLEWLGPQ AHETPIQIFG TDISEAAVEK
ARLGIYKEEA VANVSPGRLR QFFVQVAAGY QIGKSVRELC VFARQNLSSD PPFSNMDLIS
CRNVLIYLEP TLQKRVLPIF HYSLKPTGFL VLGSSESTGE FTDLFAVVDK KHKIYTRTAA
PSRLSFDFVT GDYRLARARR GGLTGEATWA GLNIQQQADR IVLNRYAPAG VLTNDRLEIL
QFRGETGAYL RPAPGEPSFN LLKMARPGLL PELHTAIYQA KSQEGAVEKA GLRVEGNDGP
RHIRIVVIAF KVPPADERYF LVLFETMDPV MPAAPEARHR HDSDQRIDPE PEISRLRQEL
TIVRQELVHT QAYLQSIIEE QEATNQSLTT ANEEILSSNE ELQSTNEELQ TAKEEIQSAN
EELRTTNEEL QSRNLEARQV NNDLLNLLSN VNIPILMLTN DLRIRRFTPA AQRLFNLIAT
DVGRSLSDIR LNFHAPDLEE SLLEVIDTLS PKEREVQDLE GYWYLLRIRP YRTVDHQIDG
VVLALVDIDA LKNSAQLLEA ARIYAESIVE TVRGPLLVLD SDLRVRTANR AFYQTFQTVP
AQTEGQRLFE LAGGQWDIPR LRLMLENLLL HNAQLLDYEV EHDFENVGRR VMLLNAQEIL
APEQDRLILL ALEDITEQKR TQQSQQMALQ KEYELNELKS RLIAMTSHEF RTPLSTIILS
TQLLSSDSPH QSAQKRLKQQ QRIERAIEQM TDLLDGILSI GQAEIDQVQI RRVPLDLESF
CRQLVEEMQA APGGAHRPAF ESAGQCRGAN LDAVMLRQIL SNLLTNALKY SAPDSTVRLQ
LACRDGQAVF TVVDEGIGIA VEDQERLFEP FYRGRNVANI PGSGLGLAIV RRLVELLKGR
LAFESRPQQG TTFTVALPLE EPADD
//
