CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018435
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) 
Protein Synonyms/Alias
 Ditrans,polycis-undecaprenylcistransferase; Undecaprenyl diphosphate synthase; UDS; Undecaprenyl pyrophosphate synthase; UPP synthase 
Gene Name
 uppS 
Gene Synonyms/Alias
 STM0221 
Created Date
 July 27, 2013 
Organism
 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) 
NCBI Taxa ID
 99287 
Lysine Modification
Position
Peptide
Type
References
36RWAKKQGKIRAFGHKacetylation[1]
43KIRAFGHKAGAKSVRacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 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). 
Sequence Annotation
 REGION 26 29 Substrate binding (By similarity).
 REGION 70 72 Substrate binding (By similarity).
 REGION 199 201 Substrate binding (By similarity).
 ACT_SITE 25 25 By similarity.
 ACT_SITE 73 73 Proton acceptor (By similarity).
 METAL 25 25 Magnesium (By similarity).
 METAL 198 198 Magnesium (By similarity).
 METAL 212 212 Magnesium (By similarity).
 BINDING 30 30 Substrate (By similarity).
 BINDING 38 38 Substrate (By similarity).
 BINDING 42 42 Substrate (By similarity).
 BINDING 74 74 Substrate (By similarity).
 BINDING 76 76 Substrate (By similarity).
 BINDING 193 193 Substrate (By similarity).  
Keyword
 Cell shape; Cell wall biogenesis/degradation; Complete proteome; Magnesium; Metal-binding; Peptidoglycan synthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 252 AA 
Protein Sequence
MLSATQPVSE NLPAHGCRHV AIIMDGNGRW AKKQGKIRAF GHKAGAKSVR RAVSFAANNG 60
IDALTLYAFS SENWNRPAQE VSALMELFVW ALDSEVKSLH RHNVRLRIIG DISRFNSRLQ 120
ERIRKSEALT AHNTGLTLNI AANYGGRWDI VQGVRQLAEQ VQAGVLRPDQ IDEERLGQQI 180
CMHELAPVDL VIRTGGEHRI SNFLLWQIAY AELYFTDVLW PDFDEQDFEG ALHAFANRER 240
RFGGTEPGDD KA 252 
Gene Ontology
 GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
Interpro
 IPR001441; UPP_synth-like.
 IPR018520; UPP_synth-like_CS. 
Pfam
 PF01255; Prenyltransf 
SMART
  
PROSITE
 PS01066; UPP_SYNTHASE 
PRINTS