ID A0A139X199_9CYAN Unreviewed; 1416 AA.
AC A0A139X199;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=WA1_37270 {ECO:0000313|EMBL:KYC38430.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC38430.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC38430.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC38430.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC38430.1}.
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DR EMBL; ANNX02000041; KYC38430.1; -; Genomic_DNA.
DR RefSeq; WP_017750169.1; NZ_KQ976354.1.
DR STRING; 128403.WA1_37270; -.
DR OrthoDB; 9799157at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00448; REC; 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; SSF52172; CheY-like; 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.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..207
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 223..495
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1031..1250
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1283..1403
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 723..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1334
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1416 AA; 158291 MW; 631AF32B6ABE108D CRC64;
MNDPRSDEPQ STAKEETVEE QLEKNQELFP IVGIGASAGG LAAFTELLGH LPTDTGMGFV
LIQHLDPESK SWLSEILART TEMPVIEVQD GMSVEPNHVY VIPPNTKMTL AQGRLRLSPR
EKTRGMYMPV DVFFRSSAMH RGNKAIGIVL SGMDGDGAQG LKAIKAAGGI TFAQCEATAK
FTGMPNTAVA TGDVDFILPP RAIGEKLANI SRHPYVTRPD LVETVEELSQ SENALQNIFK
LLRAAKGIDF THYKHTTLKR RILRRMVLYR LEKLENYVTY LQNNPAEVEA LFQDFLIHVT
SFFRDSNAFE ALKNQVFPSI MQNRSPDEPI RIWVAGCSTG EEVYSIAICL LEFLDDLQSS
PTIQIFGTDI SDFAIERARS ATYIPSLVDK ISPERLRRFF DKVEGGYQVS KLIRQMCVFA
KQNLIGDPPF SHLDLISCRN LLIYLGSALQ KKVIPLFHYS LKPTGFLLLG TSESTGDYSD
LFTLIDKKQK IYSRKLTASR LNFDFFTSNY LAQKVNDEAR DSDVGEGLDL EKEADRIVWN
KYVPPGVIIN SALEILQFRG KTSPYLAPAP GKPSFSLLKM AQASLRLDLR TAINQAKRLD
IPVRKEGIQL TTKEQLRELN FEVIPFQVPP SQERYFLVLF EDVQASAIPQ SADDDRRVKP
SRGKQTATKQ ELIQLKQELA ANKQELTATK EYLQSIIREQ EATNQELMTA NEEILSSNEE
IQSTNEELET AKEETQSTNE ELSTTNDELQ SRIQELNKVN SDIRNLLISV NIPIIILAKD
LTIRRFTPMA QKILNLIPTD VGRPLNHIKP NINVPNLEQT ILEVIDTLVI KEQEVQDTEG
HWYDLRIRPY KNLENQIDGA VMVLVDIDAL KSSSEQLKES RDYAEAIVET IQEPLLVLDA
NLRVVTANQY FYEIFLVSKA ETEYRSIFEL GNGQWDIPKL RSLLEEVLPQ NNQIDNFEVE
HTFEQIGRKT MLLNACKVLR ANNNEMILLT INDITESQLF EEQRNQLLIH EQSARAAAET
ANRTKDEFLS IVSHELRNPL NSILGWVGLL RNRSFDAEQT AQALEIIEQS AKSQAKLVED
LLNISRITTG KLQLNVTPID LVPVIAAAIH IARPSADAKN IQIESVLGSP DTHRVSGDPE
RLQQVLWNLL SNAIKFTPAG GQVTVKLERI GSAAQIQVID TGQGISADFL PHVFERFRQA
DSSTTRAHGG LGLGLSIVFH LVELHGGTIQ AESPGEGLGT TMTVRLPLQR MHTNTSVSTD
LLQVSRAGQE VPLDTMQTLL GLQILVVDDE AGLLELLKTI LEEYGAQVMA VTSAKEAIAR
LRANPLEYDV LLSDIGMPNE DGYALIRQVR ALNPELGGQI PAIALSAYVR EEEQRKSLAV
GFQRHIAKPV EPDQLASMIA ELARVNQMGN PEQTPD
//
