ID A0A139XAI0_9CYAN Unreviewed; 953 AA.
AC A0A139XAI0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=WA1_16925 {ECO:0000313|EMBL:KYC41718.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC41718.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC41718.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC41718.1,
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:KYC41718.1}.
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DR EMBL; ANNX02000020; KYC41718.1; -; Genomic_DNA.
DR RefSeq; WP_066612908.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139XAI0; -.
DR STRING; 128403.WA1_16925; -.
DR OrthoDB; 9799157at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
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:RHEA.
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 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; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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 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 SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50113; PAC; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 31..210
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 228..480
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 831..884
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 684..771
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 953 AA; 106627 MW; A575F25DD9242069 CRC64;
MASRRVSKKS QPNPSDGKVP TDNRQDNFNE LFPVVGIGAS AGGLEAFTQL LNYLPTNTGM
AYVIIQHMAP EQESALSQIL SRATQMSVNE AQHGMAIAPN QVYVIPPNVS MTIDQGVLKL
MPRLSTSRVF MSVDMFLLSL AEERGNKGIA VILSGADSDG AQGLEAIKAA GGVTFAQCQE
SAQVDSMPNT AIATGQVDFI LPPDQIAQKL AEISSHPYIA SQPTIKSEAD SSPTTTQEAL
AVIFNLLRKA TGLDFTHYKQ TTLNRRIQRR MLLYKLERLE NYARYLQSNP AEVMALYQDC
LIHVTSFFRD PESFNALKSL VFPVIIKDKT PGTPIRIWVA GCSTGEEAYS IAICLLEFIA
EQVPRIPIQI YATDISETAI EYARNGVYTL SQVANITPER LYRFFVQVEA GYQISKSVRE
VCVFARQNLI GDPPFSRLDL ISCRNVLIYL GNALQKKLLP IFHYGLKSTA FLMLGTSETV
GDFVDLFTLC DKKNKIYAKK LTASRPNIEL TTSSYSPTII NPQPFATEQF PNELELQREA
DRIVLNQYAP AGVVVDVNLE ILQFRGQTSP YLEPSPGRAS LNLLRMAKEE LRRELQTAIY
QAKQQKLPVK REGLQVREGG NEALLLGMPR IRQITINVIP FQIGAAQECF LVLFEDIPLV
SELPPATDDG SAPSKRKTRE PAEIARLKHE LATSREHLQS IIEEQQATNQ DLRAANEEIL
SSNEELQSTN EELETAKEEI QAANEELNTV NDELRRRTQE ATQVSNDLQN LLNSIHIPIL
MLGFDLQIRQ FTPAMEGIFN LISTDIGRPL SDITHKLNMP NLEQQILEVI RTLNLKAQEI
QDRDGHWYHL QIRPYRTIDN KIDGAVLVLI DIDDLKRSNA QLIEAKDYAN AIVETVWEPM
LVLNADLRVI TANRSFYDTF EVSLIQTEQQ LIFELGNGQW DILQYCSVKG NKG
//
