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Database: UniProt
Entry: Q32HX4_SHIDS
LinkDB: Q32HX4_SHIDS
Original site: Q32HX4_SHIDS 
ID   Q32HX4_SHIDS            Unreviewed;       249 AA.
AC   Q32HX4;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Lipid A 1-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01945};
DE            EC=2.7.4.29 {ECO:0000256|HAMAP-Rule:MF_01945};
DE   AltName: Full=Kdo(2)-lipid A phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01945};
DE   AltName: Full=Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01945};
GN   Name=lpxT {ECO:0000256|HAMAP-Rule:MF_01945};
GN   OrderedLocusNames=SDY_0905 {ECO:0000313|EMBL:ABB61081.1};
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB61081.1, ECO:0000313|Proteomes:UP000002716};
RN   [1] {ECO:0000313|EMBL:ABB61081.1, ECO:0000313|Proteomes:UP000002716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197 {ECO:0000313|EMBL:ABB61081.1,
RC   ECO:0000313|Proteomes:UP000002716};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Involved in the modification of the lipid A domain of
CC       lipopolysaccharides (LPS). Transfers a phosphate group from
CC       undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-
CC       diphosphate. Contributes to the recycling of undecaprenyl
CC       phosphate (C55-P). {ECO:0000256|HAMAP-Rule:MF_01945}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A + di-
CC         trans,octa-cis-undecaprenyl diphosphate = (Kdo)2-lipid A 1-
CC         diphosphate + di-trans,octa-cis-undecaprenyl phosphate;
CC         Xref=Rhea:RHEA:45468, ChEBI:CHEBI:58405, ChEBI:CHEBI:58540,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:85271; EC=2.7.4.29;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01945};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01945}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01945}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01945}. Note=Transferase activity takes place on the
CC       periplamic side of the inner membrane. {ECO:0000256|HAMAP-
CC       Rule:MF_01945}.
CC   -!- SIMILARITY: Belongs to the LpxT phosphotransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01945}.
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DR   EMBL; CP000034; ABB61081.1; -; Genomic_DNA.
DR   RefSeq; WP_001110667.1; NC_007606.1.
DR   RefSeq; YP_402572.1; NC_007606.1.
DR   EnsemblBacteria; ABB61081; ABB61081; SDY_0905.
DR   GeneID; 3799315; -.
DR   KEGG; sdy:SDY_0905; -.
DR   PATRIC; fig|300267.13.peg.1046; -.
DR   HOGENOM; HOG000282674; -.
DR   KO; K19803; -.
DR   OMA; RSFPGDH; -.
DR   BioCyc; SDYS300267:G1G4A-997-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:InterPro.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01945; Lipid_A_LpxT; 1.
DR   InterPro; IPR032908; LpxT.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002716};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002716};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01945};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01945}.
FT   TRANSMEM     20     37       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01945}.
FT   TRANSMEM     75     93       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01945}.
FT   TRANSMEM    105    125       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01945}.
FT   TRANSMEM    173    194       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01945}.
FT   TRANSMEM    203    224       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01945}.
FT   DOMAIN      106    222       acidPPc. {ECO:0000259|SMART:SM00014}.
SQ   SEQUENCE   249 AA;  28194 MW;  13A397623864CF9F CRC64;
     MPAFFSKIIR ENMIKNLPQI VLLNIVGLAL FLSWYIPVNH GFWLPIDADI FYFFNQKLVE
     SKAFLWLVAL TNNRAFDGCS LLAMGMLMLS FWLKENAPGR RRIVIIGLVM LLTAVVLNQL
     GQALIPVKRA SPTLTFTDIN RVSELLSVPT KDASRDSFPG DHGMMLLIFS AFMWRYFGKV
     AGLIALIIFV VFAFPRVMIG AHWFTDIIVG SMTVILIGLP WVLLTPLSDR LITFFDKSLP
     GKNKHFQNK
//
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