ID K9VDJ4_9CYAN Unreviewed; 1405 AA.
AC K9VDJ4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=Osc7112_0983 {ECO:0000313|EMBL:AFZ05544.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ05544.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ05544.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ05544.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003614; AFZ05544.1; -; Genomic_DNA.
DR STRING; 179408.Osc7112_0983; -.
DR KEGG; oni:Osc7112_0983; -.
DR PATRIC; fig|179408.3.peg.1212; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000892_2_2_3; -.
DR OrthoDB; 9799157at2; -.
DR Proteomes; UP000010478; 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:UniProtKB-EC.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; PF13596; PAS_10; 1.
DR Pfam; PF13188; PAS_8; 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; SM00091; PAS; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050,
KW ECO:0000313|EMBL:AFZ05544.1}; Kinase {ECO:0000313|EMBL:AFZ05544.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AFZ05544.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ05544.1}.
FT DOMAIN 31..210
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 244..499
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1032..1248
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1282..1402
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 687..753
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"
FT MOD_RES 1333
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1405 AA; 155327 MW; 01F0902A75428438 CRC64;
MTSPQLSPEN TPESIAPAAL DREQLTETDA PFPIVGIAAS AGGLEAFTQL LSHLPSDTGM
AFVLIQHLAP DHKSLLSEIL ARTTQMPVNE VEDGVAVEPN QVYVIPPNTK MVLSKGVLQL
SPREKIYGKY LPGDAFFTSL AIDRGHKAIA VVLSGGDGDG SLGLNAIKAA GGMTFAQCQD
TAKFDSMPIT AVATGNVDFV LPPEKIAEEL ANYSHNPLLT GPLAMTKVEE SPEQGDALAT
IFALLKSTTG VDFSHYKPTT IARRIQRRMV LYKLESLDDY AQHLRHNSAE VTALYEEILI
HVTSFFRDPE AFEKLKELVF PTITQNKSAE TPIRIWVAGC STGEEVYSIA ICLLEFLGDR
AIQPPIQIFA TDIGEQAIGK ARSGVYSENQ MVDVSPERRT GYFIAQEEGS YRISKAVREL
CVFARQDLGS DPPFSNLDLV SCRNVLIYLG ESLQKKLMPI FHYSLNPNGF LLLGTSESTG
KFSYLFTSVD KNSKIYAKNL TATRPTFSFT PSSYPVAKAR ERQEVKENLT NSFDLQRETD
QLILNRYALA GVVVNDLMNI LQVRGDINPY FRLAFGTPDL NLLTMAREGL LLELRTAIYQ
AQTQNVTVRK EGVSVVESAG RSSIVNFEVI PFQPQAVEGR YFLVLLEQAS PPMLKLTPLP
SESFEQADLV REIDLLRQAL ATAYQDKTAV QTQLQAVIQE HENLNQDIKI ANEEILSSNE
ELQSTNEELE TAKEEIQATN EELTTTNEEL RSRNIEQSLV NNDLINLLSS INIPILMLTN
DLQIRRFTPT AQQIFSVIPT DVGRPFSDIR STLNVPGLEQ MILEVIDTLQ TKEQEIQTLS
GYWYNLRIRP YRTTENQIDG VVMVLLDIDA LKRSARTLEE ARNYAETIVE TVQTPLVALD
ANFRVNKANR AFYETFQISS SETAQSSLFE LGNGQWNIPQ LRWILEDILV SDVQLENFEL
THLFEKIGQK TMLLNACKLQ REDQALMILL SIEDITERKQ FEKVRSQLFE HEQLARQQAE
TANRAKDEFL ANLSHELRNP LTPILGWSQI LRSGKLKGVA VTKALEVIDR SARAQSQLIE
DILDISRITS GKLQLCICPI DLRLVVQAAV EGVQLSAEAK NIQIVSELIS TSVLGDINRL
QQVVWNLLSN AIKFTPAGGR VEILLSAIDN HAQLRVSDTG KGIEAQFLPY IFDRFHQGDS
SSVKANQGLG LGLSIVRHLV ELHGGTVQAE SPGEGQGTTM TVRLPLRSLP QELTSAIDLK
STALAGPLNA SSDRVPSLEG LHILAVDDQI DTRDFLQFVL EGYGAEVLAV ASARSAIAAL
TENPGRYDVL ISDLGMPEED GFFLIREVRA LAAEAGGEIP AAALTAYAGN KEREMAIEAG
FQRHMVKPIE PVVLGLMVAN LVGRF
//
