WBDD2_ECOLX
ID WBDD2_ECOLX Reviewed; 708 AA.
AC Q47592;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=O-antigen chain terminator bifunctional methyltransferase/kinase WbdD {ECO:0000250|UniProtKB:J7I4B7};
DE Includes:
DE RecName: Full=3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase {ECO:0000250|UniProtKB:J7I4B7};
DE EC=2.1.1.294 {ECO:0000250|UniProtKB:J7I4B7};
DE Includes:
DE RecName: Full=Polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase {ECO:0000250|UniProtKB:J7I4B7};
DE EC=2.7.1.181 {ECO:0000250|UniProtKB:J7I4B7};
GN Name=wbdD {ECO:0000250|UniProtKB:J7I4B7};
GN Synonyms=ORF708 {ECO:0000312|EMBL:BAA07749.1};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000312|EMBL:BAA07749.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O9:K31-:H- / F719;
RX PubMed=8162191; DOI=10.1099/13500872-140-1-59;
RA Sugiyama T., Kido N., Komatsu T., Ohta M., Jann K., Jann B., Saeki A.,
RA Kato N.;
RT "Genetic analysis of Escherichia coli 09 rfb: identification and DNA
RT sequence of phosphomannomutase and GDP-mannose pyrophosphorylase genes.";
RL Microbiology 140:59-71(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O9:K31-:H- / F719;
RX PubMed=7536735; DOI=10.1128/jb.177.8.2178-2187.1995;
RA Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T.,
RA Kato N., Jann K.;
RT "Expression of the O9 polysaccharide of Escherichia coli: sequencing of the
RT E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and
RT evidence for an ATP-binding cassette transport system.";
RL J. Bacteriol. 177:2178-2187(1995).
CC -!- FUNCTION: Regulates the length of the LPS O-antigen polysaccharide
CC chain. Stops the polymerization of the chain by phosphorylating and
CC then methylating the phosphate on the terminal sugar. This terminal
CC modification is essential for export of the O-antigen across the inner
CC membrane. WbdD is also required for correct localization of the WbdA
CC mannosyltransferase. {ECO:0000250|UniProtKB:J7I4B7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-
CC alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-
CC adenosyl-L-methionine = 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-
CC Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36639, Rhea:RHEA-
CC COMP:9559, Rhea:RHEA-COMP:9560, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74008, ChEBI:CHEBI:74009; EC=2.1.1.294;
CC Evidence={ECO:0000250|UniProtKB:J7I4B7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-
CC alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-
CC trans,octa-cis-undecaprenyl diphosphate + ATP = 3-O-phospho-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-
CC undecaprenyl diphosphate + ADP + H(+); Xref=Rhea:RHEA:40371,
CC Rhea:RHEA-COMP:9558, Rhea:RHEA-COMP:9559, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:74008, ChEBI:CHEBI:74010,
CC ChEBI:CHEBI:456216; EC=2.7.1.181;
CC Evidence={ECO:0000250|UniProtKB:J7I4B7};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000250|UniProtKB:J7I4B7}.
CC -!- SUBUNIT: Interacts with WbdA. {ECO:0000250|UniProtKB:J7I4B7}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:J7I4B7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:J7I4B7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:J7I4B7}.
CC -!- SIMILARITY: Belongs to the WbdD family. {ECO:0000305}.
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DR EMBL; D43637; BAA07749.1; -; Genomic_DNA.
DR PIR; I76774; I76774.
DR AlphaFoldDB; Q47592; -.
DR SMR; Q47592; -.
DR BioCyc; MetaCyc:MON-21644; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Coiled coil; Kinase;
KW Lipopolysaccharide biosynthesis; Membrane; Methyltransferase;
KW Nucleotide-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..708
FT /note="O-antigen chain terminator bifunctional
FT methyltransferase/kinase WbdD"
FT /id="PRO_0000430677"
FT REGION 1..210
FT /note="Methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT REGION 211..459
FT /note="Kinase"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT REGION 601..669
FT /note="Required for membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT REGION 687..708
FT /note="Required for localizing WbdA to the membrane"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT COILED 485..594
FT /evidence="ECO:0000255"
FT BINDING 16..17
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 82..87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 108..111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 241..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 309..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
FT BINDING 369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:J7I4B7"
SQ SEQUENCE 708 AA; 81571 MW; 7416BE1AA24C4CB9 CRC64;
MTKDLNTLVS ELPEIYQTIF GHPEWDGDAA RDCNQRLDLI TEQYDNLSRA LGRPLNVLDL
GCAQGFFSLS LASKGATIVG IDFQQENINV CRALAEENPD FAAEFRVGRI EEVIAALEEG
EFDLAIGLSV FHHIVHLHGI DEVKRLLSRL ADVTQAVILE LAVKEEPLYW GVSQPDDPRE
LIEQCAFYRL IGEFDTHLSP VPRPMYLVSN HRVLINDFNQ PFQHWQNQPY AGAGLAHKRS
RRYFFGEDYV CKFFYYDMPH GILTAEESQR NKHELHNEIK FLTQPPAGFD APAVLAHGEN
AQSGWLVMEK LPGRLLSDML AAGEEIDREK ILGSLLRSLA ALEKQGFWHD DVRPWNVMVD
ARQHARLIDF GSIVTTPQDC SWPTNLVQSF FVFVNELFAE NKSWNGFWRS APVHPFNLPQ
PWSNWLYAVW QEPVERWNFA LLLALFEKKA KLPSAEQQRG ATEQWIIAQE TVLLELQSRG
RNESAGSEAL RGQIHTLEQQ MAQLQSAQDA FVEKAQQPVE VSHELTWLGE NMEQLAALLQ
TAQAHAQADV QPELPPETAE LLQRLEAANR EIHHLSNENQ QLRQEIEKIH RSRSWRMTKG
YRYLGLQIHL LRQYGFVQRC KHFIKRVLRF VFSFMRKHPQ VKHTAVNGLH KLGLYQPAYR
LYRRMNPLPH SQYQADAQIL SQTELQVMHP ELLPPEVYEI YLKLTKNK
