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Database: UniProt
Entry: Q87T58_VIBPA
LinkDB: Q87T58_VIBPA
Original site: Q87T58_VIBPA 
ID   Q87T58_VIBPA            Unreviewed;       352 AA.
AC   Q87T58;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=lipopolysaccharide heptosyltransferase II {ECO:0000256|ARBA:ARBA00044042};
DE            EC=2.4.99.24 {ECO:0000256|ARBA:ARBA00044042};
GN   OrderedLocusNames=VP0212 {ECO:0000313|EMBL:BAC58475.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC58475.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC58475.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-L-glycero-beta-D-manno-heptose + an L-alpha-D-Hep-(1->5)-
CC         [alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-lipid A = ADP + an L-alpha-D-Hep-
CC         (1->3)-L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-lipid
CC         A + H(+); Xref=Rhea:RHEA:74071, ChEBI:CHEBI:15378, ChEBI:CHEBI:61506,
CC         ChEBI:CHEBI:193068, ChEBI:CHEBI:193069, ChEBI:CHEBI:456216;
CC         EC=2.4.99.24; Evidence={ECO:0000256|ARBA:ARBA00043830};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 9 family.
CC       {ECO:0000256|ARBA:ARBA00043995}.
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DR   EMBL; BA000031; BAC58475.1; -; Genomic_DNA.
DR   RefSeq; NP_796591.1; NC_004603.1.
DR   RefSeq; WP_005466240.1; NC_004603.1.
DR   AlphaFoldDB; Q87T58; -.
DR   GeneID; 1187679; -.
DR   KEGG; vpa:VP0212; -.
DR   PATRIC; fig|223926.6.peg.204; -.
DR   eggNOG; COG0859; Bacteria.
DR   HOGENOM; CLU_038371_7_0_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd03789; GT9_LPS_heptosyltransferase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002201; Glyco_trans_9.
DR   InterPro; IPR011910; RfaF.
DR   NCBIfam; TIGR02195; heptsyl_trn_II; 1.
DR   PANTHER; PTHR30160:SF7; ADP-HEPTOSE--LPS HEPTOSYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR30160; TETRAACYLDISACCHARIDE 4'-KINASE-RELATED; 1.
DR   Pfam; PF01075; Glyco_transf_9; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAC58475.1}.
SQ   SEQUENCE   352 AA;  39315 MW;  14D11107BF4742E9 CRC64;
     MKKILIIGPA WVGDMVMSQS LYITLKQLHP ESQIDVIAPG WCKPILERMP EIHQAIEMPI
     GHGEFNLLGR REIGKSLREK QYDHAYILPK SAKSALIPWF ANIPLRTGWK GEMRYGLLND
     LRPNMKSFQY MVERYVALAY SKSEMVDSSS LGGLDTLPRP SLSLNKEEQQ TTINKFNLDQ
     KRPAVGLCPG AEFGPAKKWP ETHYAEVAAQ MCKTGHQVWL FGSQKDLETC NNIRALIPTQ
     FHEHIHVLAG QTSLIEAVDL LAACKTVVAN DSGLMHVAAA VGCNVVAVYG STSPKYTPPL
     AEKVEMVHTD IDCRPCFKRE CQYQHLKCLT ELSPKQVLDS IQKLEAIATS SC
//
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