ID A0A0N9ZFN8_9RHOB Unreviewed; 1180 AA.
AC A0A0N9ZFN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Chemotaxis protein methyltransferase CheR {ECO:0000313|EMBL:ALI54527.1};
DE EC=2.1.1.80 {ECO:0000313|EMBL:ALI54527.1};
GN ORFNames=IMCC12053_579 {ECO:0000313|EMBL:ALI54527.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI54527.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI54527.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI54527.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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; CP012023; ALI54527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N9ZFN8; -.
DR STRING; 1397108.IMCC12053_579; -.
DR KEGG; cmar:IMCC12053_579; -.
DR PATRIC; fig|1397108.4.peg.598; -.
DR Proteomes; UP000064920; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase 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: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; 3.30.565.10; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
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; PF07536; HWE_HK; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
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.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ALI54527.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000064920};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALI54527.1}.
FT DOMAIN 1..189
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 211..466
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 782..833
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 841..892
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 476..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 632..719
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 824..851
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1180 AA; 132307 MW; A67D644216631F1E CRC64;
MTVIPIVGIG ASAGGLEALQ VMMSSTPLDT GAAYVIVQHF APTQKSVLHE LLQHETELHV
SQVLDNETIV PNQVYVVPPG HVADIDGDIL HLTARDPSDT QHKPIDAFFK SLARERGRDA
YCVILSGTGS DGSQGLREIK AVGGVAFVQD RKGARFAGMP DSAIETGLVD FILPAAQIPV
RIDDVIKRRA HVPSKEGSSR LQAEIHSALP RFFERLEQAA GHDFGDYKPG TLVRRIERRM
AALRLKDVDD FLAVLEDDDE AKLLAQDFLI GVTEFFRDPE AFEALRVLAI QPILEHNEKT
IRVWVPSCST GEEVYSLAML FIEEMEAVGD RRPLQVFGTD IDTPALMSAR YGLYSQSAVE
SLTEERRNTF FQPENGQYRT IPRLRECCVF APHNLLQDPP FSRLDLISCR NLMIYLSANL
QKQVIPRFHF ALRGRGNLFL GPSETLVGEE KLFETLDKSW RIFRKNTDVR ASYSAIDETP
RQPTPLQPFQ TMPPNKVSQS TENSRESTVE RTYLRHFASP FALVSKTGEI LYLSQSMTGF
VQPSSGAPSS MIDSYLMREL RFPVRTALAQ AVDTGHSARV DSVVLLDDKD RRIFDIEVAP
SGTDFILIMT QVRAMDGVDL TDMMSERDIE SRDILETENA QLRRQLAMTL QQFDTSGQEL
KSGNEELMSM NEELQSSNEE LETSREELEA INEELETVNA ELKENNRLLT RANSDLKNLF
ESTDLAVLFV DRAFCVRNFT PATSDIFGIK SRDIGRPIDD LSSRIVYPDL KSDAQTVDTT
LQVLEREFAI EDTQQTYMLR MKPYRTTDNR LDGYVLSFVD ITQRKAYENS LKENERALAR
QYAELEKLYD TIPVGLSLMD RDLRWVRINS SLADMNGFSV EEHIGRTFRD LLPDFEDFTG
AIYEEVFATG EPVFGLTIDG ETPAAPGVKR HFIADFYPLW QEDKVFAVGS CVREVTEQTK
IVKRVRAQNS QQKLLMGELQ HRVKNTLSVI SSISQLLLVG VDDPAVYHAR LEDRLSAISR
THDLLTDANW TTTALSNIVA NEAKPFETNS HARVNMSGPD IQLTAEQALS VGMAIHELIT
NAAKYGALSR PKGFVEVVTR IHKKDGVAHA HLTWTEHNGP KITKAPKHTG FGSLVLERVL
KTDLAADVTC DYRKDGLFFE LDFALAKIED DSALISANDV
//
