CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003154
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division protein FtsZ 
Protein Synonyms/Alias
  
Gene Name
 ftsZ 
Gene Synonyms/Alias
 sfiB; sulB; b0095; JW0093 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
133LTVAVVTKPFNFEGKacetylation[1]
140KPFNFEGKKRMAFAEacetylation[1]
141PFNFEGKKRMAFAEQacetylation[1]
155QGITELSKHVDSLITacetylation[1]
167LITIPNDKLLKVLGRacetylation[1]
170IPNDKLLKVLGRGISacetylation[1]
319ATGIGMDKRPEITLVacetylation[1]
329EITLVTNKQVQQPVMacetylation[1]
352APLTQEQKPVAKVVNacetylation[1]
356QEQKPVAKVVNDNAPacetylation[1, 2]
367DNAPQTAKEPDYLDIacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. Polymerization and bundle formation is enhanced by CbeA. 
Sequence Annotation
 NP_BIND 103 111 GTP (Potential).  
Keyword
 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Nucleotide-binding; Reference proteome; Septation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 383 AA 
Protein Sequence
MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR KTAVGQTIQI 60
GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI AAGMGGGTGT GAAPVVAEVA 120
KDLGILTVAV VTKPFNFEGK KRMAFAEQGI TELSKHVDSL ITIPNDKLLK VLGRGISLLD 180
AFGAANDVLK GAVQGIAELI TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA 240
EMAISSPLLE DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP 300
DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE QKPVAKVVND 360
NAPQTAKEPD YLDIPAFLRK QAD 383 
Gene Ontology
 GO:0032153; C:cell division site; IEA:HAMAP.
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0043234; C:protein complex; IEA:InterPro.
 GO:0005525; F:GTP binding; IDA:EcoliWiki.
 GO:0003924; F:GTPase activity; IDA:EcoliWiki.
 GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IMP:EcoliWiki.
 GO:0043093; P:cytokinesis by binary fission; IEA:HAMAP.
 GO:0051258; P:protein polymerization; IDA:EcoliWiki. 
Interpro
 IPR000158; Cell_div_FtsZ.
 IPR020805; Cell_div_FtsZ_CS.
 IPR024757; FtsZ_C.
 IPR008280; Tub_FtsZ_C.
 IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
 IPR003008; Tubulin_FtsZ_GTPase. 
Pfam
 PF12327; FtsZ_C
 PF00091; Tubulin 
SMART
 SM00864; Tubulin
 SM00865; Tubulin_C 
PROSITE
 PS01134; FTSZ_1
 PS01135; FTSZ_2 
PRINTS
 PR00423; CELLDVISFTSZ.