ID A0A150WLM5_BDEBC Unreviewed; 1613 AA.
AC A0A150WLM5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=AZI86_11970 {ECO:0000313|EMBL:KYG64909.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG64909.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG64909.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG64909.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-2016) 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};
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:KYG64909.1}.
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DR EMBL; LUKE01000002; KYG64909.1; -; Genomic_DNA.
DR RefSeq; WP_061835420.1; NZ_LUKE01000002.1.
DR Proteomes; UP000075320; 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: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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 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; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 4.
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); 4.
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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000075320};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..197
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 216..471
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 840..911
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1040..1092
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1239..1461
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1488..1605
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 654..727
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1537
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1613 AA; 181137 MW; D9DC70654E0DED64 CRC64;
MPSKTPVENS PKRLIGVGAS AGGLEALTSL ISNISKDFSD TLIVAQHLAP HGKSMLVELL
AKQSKIPVIA ATHEARLKKG HIYIVPPNMN IRVDDKSLFL EESDIDKRPI PSIDTFFISL
GQFWRENGVG IILSGTGSDG SEGIRAIHHA GGLTLAQDGF SAKYDGMPQA AIDTACVDVI
LSPDEMGRTL ASLIEEHIQE RKADLLNTPE WKECLKILID KTGSDFSQYK PSTLQRRLWR
RVLQVHCKSL SEYLAYLKRT PGEVGILSQE LLVSVTSFFR DAEVFEELGR ILETQISTKR
AGEDLRIWVA GCATGEEAYS LAILACEALE KIHRNVPVKI FATDLDQDAI AEGRKGVYDS
DSLLALPKDY LRKYFTKLSD GRFELQKRIR DMVVFAKQDM IQNPPFVRLD LVTCRNVLIY
FEPELQKRVL EIFHFALTNS GYLCLGKSES PGSDSTFFET FDKKLKIYKK NDVASSLQMN
RFSTTSKAEF IPARRRPESN GPSLLEKGLL RILRDYGHSG VIVDKDLNMV QVLGDISEFA
SFSASQSDSR LISLLPKQVG IELPMLLKRA TDDMNIHFSH WYTSSGKKTQ FRMAVRMMSE
ESSRDARNSL FLISFESRRE DVSTAPAGRS LSADELPSHV LEMEQELFAT REHLQTVIEE
LGVANEELQS LNEELSSANE ELQSTNEELE TTNEELQSGN EELTTVNEEL NMKSQQLRET
NTSLENIQES IGAGLVVVDK SGQVVRFNQE VLKIFALNTS HIGKSLAQVS AYLELPDFQK
HVNEAIEQGK TSETVCEGAN AVYQMRCQPF YDENRKIVGA TLVFIDETAI TKTRQKLQRS
ETQLRAILES FTGPVSMKDP HGRYLMVNST FLKFFNLSMD QVLGRTDQDL FDNAMASAMR
KADLEVMFRG DPLRQSEDVL DRHGKKRVLY SSRFPLYEGR QDTPYAIGMI AVDITAQTEM
QAQLAESESR YKALIEDQAV FVCRMTPSGE LIYANNLFEV HFSDAGRSVE GSFFQNFLPR
HDMGKVQGDL SSISTRQPIM QSEYRVYRKN GVARWIRWIL KGIFDASGEV LEIQAIGFDI
TDYRTQTDRL LEKEAIFSTI LGNTSDMAVI LHRQENEFVP EYFNKIAEEI LKSEGPLLGR
PLSQTRAPER VTRLYEMFEY ALNTNESVTF EDHWFAGTRE LYLLYTVVPL RSSVVSDGVD
RVAVLCKDIS AHKVIEHDLR IAKEAAEVAN EAKSDFLASM SHELRTPLNV VLGMSTLLSE
THLDEDQKEF VGSIDRSGKA LLSLIEDILD ISKIESGKIK LSAETFDLRE LVKESVRMFE
SSASSKGIAL ELAMDFPSEE LVVGDPGRLR QVLVNLVGNA LKFTDKGQVT VTVRPGYYDF
AGEKEYYFEV KDTGIGIKKQ DHGKIFQKFS QVESGHSRRF GGSGLGLVIS RQIAEMMKGT
MGFDSEEGHG STFWFSVKLH SAAQSEIRAK QRRQQLMRVD LDDPTELHVL AVDDNKESLN
VIRLFIERLG HKVYPAGRGL EAIQVLKANP IDVVLMDVQM PGMDGYETTR MIRKDPTIPS
QLPIIALTAN AMSGDAEKCL QAGMNDYLTK PIRIDVLKEM LSRWSLHLKG KGE
//
