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Database: UniProt
Entry: K8WV45_9GAMM
LinkDB: K8WV45_9GAMM
Original site: K8WV45_9GAMM 
ID   K8WV45_9GAMM            Unreviewed;       326 AA.
AC   K8WV45;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Lipopolysaccharide heptosyltransferase 1 {ECO:0000256|ARBA:ARBA00044190};
DE            EC=2.4.99.23 {ECO:0000256|ARBA:ARBA00044041};
DE   AltName: Full=ADP-heptose:lipopolysaccharide heptosyltransferase I {ECO:0000256|ARBA:ARBA00044330};
GN   ORFNames=OO7_01291 {ECO:0000313|EMBL:EKT61297.1};
OS   Providencia sneebia DSM 19967.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT61297.1, ECO:0000313|Proteomes:UP000010290};
RN   [1] {ECO:0000313|EMBL:EKT61297.1, ECO:0000313|Proteomes:UP000010290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT61297.1,
RC   ECO:0000313|Proteomes:UP000010290};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-L-glycero-beta-D-manno-heptose + an alpha-Kdo-(2->4)-
CC         alpha-Kdo-(2->6)-lipid A = ADP + an L-alpha-D-Hep-(1->5)-[alpha-Kdo-
CC         (2->4)]-alpha-Kdo-(2->6)-lipid A + H(+); Xref=Rhea:RHEA:74067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:61506, ChEBI:CHEBI:176431,
CC         ChEBI:CHEBI:193068, ChEBI:CHEBI:456216; EC=2.4.99.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00043802};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 9 family.
CC       {ECO:0000256|ARBA:ARBA00043995}.
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:EKT61297.1}.
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DR   EMBL; AKKN01000002; EKT61297.1; -; Genomic_DNA.
DR   RefSeq; WP_008914152.1; NZ_CM001773.1.
DR   AlphaFoldDB; K8WV45; -.
DR   PATRIC; fig|1141660.3.peg.254; -.
DR   HOGENOM; CLU_038371_6_0_6; -.
DR   OrthoDB; 9767552at2; -.
DR   Proteomes; UP000010290; Chromosome.
DR   GO; GO:0008920; F:lipopolysaccharide heptosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009244; P:lipopolysaccharide core region 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; IPR011908; LipoPS_heptosylTferase-I.
DR   NCBIfam; TIGR02193; heptsyl_trn_I; 1.
DR   PANTHER; PTHR30160:SF19; LIPOPOLYSACCHARIDE HEPTOSYLTRANSFERASE 1; 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   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010290};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKT61297.1}.
SQ   SEQUENCE   326 AA;  36991 MW;  7C52CFFF161190A0 CRC64;
     MRVLLVKTSS MGDVLHSLPA LTDAKHALPD IQFDWVVEEN FAQIPTWHNA VNHVIPVAIR
     RWRKNWFSAP IRAERAAFRA QLQATHYDAI IDAQGLLKSA FLVTRLAHGA KHGYDRHSIR
     EPLASLFYDH RYRVSKQQHA VERIRQLFAD SLHYKCPTQK GDYGIAQHFL CSTPEQQAPY
     LIFLHSTTRD DKHWPENHWR KLIALMAPTG LRIKLPWGTE HEHQRALRLA ECFDFVEVLP
     KLTLAQVAEQ IANAQAVVSV DTGLSHLTAA LDKTNFTLFG PTDPGLIGGY GQRQHEIKSI
     NNSMESITPT AVFEQLADKK IVLGNQ
//
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