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A7MGS7 (A7MGS7_CROS8) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) HAMAP-Rule MF_01139
EC=2.5.1.31 HAMAP-Rule MF_01139
Alternative name(s):
Ditrans,polycis-undecaprenylcistransferase HAMAP-Rule MF_01139
Undecaprenyl diphosphate synthase HAMAP-Rule MF_01139
Undecaprenyl pyrophosphate synthase HAMAP-Rule MF_01139
Gene names
Name:uppS HAMAP-Rule MF_01139
Ordered Locus Names:ESA_03168 EMBL ABU78391.1
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP] EMBL ABU78391.1
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Cronobacter ›

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide By similarity. HAMAP-Rule MF_01139

Catalytic activity

(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl diphosphate. HAMAP-Rule MF_01139

Cofactor

Binds 2 magnesium ions per subunit By similarity. HAMAP-Rule MF_01139

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01139

Sequence similarities

Belongs to the UPP synthase family. HAMAP-Rule MF_01139 RuleBase RU003962

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site731Proton acceptor By similarity HAMAP-Rule MF_01139
Metal binding251Magnesium By similarity HAMAP-Rule MF_01139
Metal binding1981Magnesium By similarity HAMAP-Rule MF_01139
Metal binding2121Magnesium By similarity HAMAP-Rule MF_01139
Binding site301Substrate By similarity HAMAP-Rule MF_01139
Binding site381Substrate By similarity HAMAP-Rule MF_01139
Binding site421Substrate By similarity HAMAP-Rule MF_01139
Binding site741Substrate By similarity HAMAP-Rule MF_01139
Binding site761Substrate By similarity HAMAP-Rule MF_01139
Binding site1931Substrate By similarity HAMAP-Rule MF_01139

Sequences

Sequence LengthMass (Da)Tools
A7MGS7 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 0434C816186E1178

FASTA25228,187
        10         20         30         40         50         60 
MLSVNLPLSE NLPAHGARHV AIIMDGNGRW AKRQGKIRAF GHKAGAKSVR RAVSFAANNG 

        70         80         90        100        110        120 
IEALTLYAFS SENWNRPAQE VSALMELFVW ALDSEVKSLH RHNVRLRVIG DISRFNTRLQ 

       130        140        150        160        170        180 
DRIHKAEALT SQNTGLTLNI AANYGGRWDI IQGVQQLAAQ VQEGLLRPDQ IDEEMLSKQI 

       190        200        210        220        230        240 
CMHELAPVDL VIRTGGEHRI SNFLLWQIAY AELYFTDVLW PDFDEQDFEG ALNAFANRER 

       250 
RFGGTAPGGI DA

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894 EMBL ABU78391.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000783 Genomic DNA. Translation: ABU78391.1.
RefSeqYP_001439227.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MGS7.
SMRA7MGS7. Positions 9-239.
ModBaseSearch...

Protein-protein interaction databases

STRING290339.ESA_03168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU78391; ABU78391; ESA_03168.
GeneID5549566.
KEGGesa:ESA_03168.
PATRIC20398069. VBICroSak107175_2799.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0020.
HOGENOMHOG000006054.
KOK00806.
OMAIAYSELF.
ProtClustDBPRK10240.

Enzyme and pathway databases

BioCycCSAK290339:GJ80-3158-MONOMER.

Family and domain databases

Gene3D3.40.1180.10. 1 hit.
HAMAPMF_01139. UppS.
InterProIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERPTHR10291. PTHR10291. 1 hit.
PfamPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMSSF64005. UPP_synth. 1 hit.
TIGRFAMsTIGR00055. uppS. 1 hit.
PROSITEPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA7MGS7_CROS8
AccessionPrimary (citable) accession number: A7MGS7
Entry history
Integrated into UniProtKB/TrEMBL: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info