CPLM 1.0 - Compendium of Protein Lysine ModificationTag | Content |
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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 |
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36 | RWAKKQGKIRAFGHK | acetylation | [1] | 43 | KIRAFGHKAGAKSVR | acetylation | [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 | | Pfam | | SMART | | PROSITE | | PRINTS | |
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