(data stored in SCRATCH zone)

SWISSPROT: B7UIL9_ECO27

ID   B7UIL9_ECO27            Unreviewed;       253 AA.
AC   B7UIL9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.31 {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Ditrans,polycis-undecaprenylcistransferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            Short=UDS {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            Short=UPP synthase {ECO:0000256|HAMAP-Rule:MF_01139};
GN   Name=ispU {ECO:0000313|EMBL:CAS07727.1};
GN   Synonyms=uppS {ECO:0000256|HAMAP-Rule:MF_01139};
GN   OrderedLocusNames=E2348C_0179 {ECO:0000313|EMBL:CAS07727.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07727.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07727.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to
CC       yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl
CC       diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of
CC       glycosyl carrier lipid in the biosynthesis of bacterial cell wall
CC       polysaccharide components such as peptidoglycan and
CC       lipopolysaccharide. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
CC         = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate;
CC         Xref=Rhea:RHEA:27551, ChEBI:CHEBI:33019, ChEBI:CHEBI:58405,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.31;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01139};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01139}.
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DR   EMBL; FM180568; CAS07727.1; -; Genomic_DNA.
DR   SMR; B7UIL9; -.
DR   EnsemblBacteria; CAS07727; CAS07727; E2348C_0179.
DR   KEGG; ecg:E2348C_0179; -.
DR   HOGENOM; HOG000006054; -.
DR   KO; K00806; -.
DR   OMA; FDRRDLW; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR10291; PTHR10291; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; SSF64005; 1.
DR   TIGRFAMs; TIGR00055; uppS; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIL9.
DR   SWISS-2DPAGE; B7UIL9.
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01139}.
FT   REGION       27     30       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   REGION       71     73       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   REGION      200    202       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   ACT_SITE     26     26       {ECO:0000256|HAMAP-Rule:MF_01139}.
FT   ACT_SITE     74     74       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL        26     26       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL       199    199       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL       213    213       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      31     31       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      39     39       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      43     43       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      75     75       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      77     77       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING     194    194       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
SQ   SEQUENCE   253 AA;  28444 MW;  73DC9534C14CA7B9 CRC64;
     MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV RRAVSFAANN
     GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL HRHNVRLRII GDTSRFNSRL
     QERIRKSEAL TAGNTGLTLN IAANYGGRWD IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH
     VCMHELAPVD LVIRTGGEHR ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE
     RRFGGTEPGD ETA
//

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