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Protein

Peptidoglycan synthase FtsI

Gene

ftsI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates.

Catalytic activityi

(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.

Pathway: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei307 – 3071Acyl-ester intermediate

GO - Molecular functioni

  • penicillin binding Source: EcoliWiki
  • peptidoglycan glycosyltransferase activity Source: EcoliWiki

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: EcoliWiki
  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
  • regulation of cell shape Source: UniProtKB-KW
  • response to antibiotic Source: UniProtKB-KW
  • response to drug Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance, Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10341-MONOMER.
ECOL316407:JW0082-MONOMER.
MetaCyc:EG10341-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidoglycan synthase FtsI (EC:2.4.1.129)
Alternative name(s):
Penicillin-binding protein 3
Short name:
PBP-3
Peptidoglycan glycosyltransferase 3
Gene namesi
Name:ftsI
Synonyms:pbpB
Ordered Locus Names:b0084, JW0082
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10341. ftsI.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei19 – 3921HelicalSequence AnalysisAdd
BLAST
Topological domaini40 – 577538PeriplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell division site Source: EcoliWiki
  • integral component of plasma membrane Source: EcoliWiki
  • intrinsic component of plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071S → A or T: Unable to bind penicillin. 1 Publication
Mutagenesisi307 – 3071S → C: Still able to bind penicillin. 1 Publication
Mutagenesisi361 – 3611N → S in PBPBR1; obtained after selection for increased resistance to cephalexin, causes a change in the shape of the cell: The polar caps are pointed. 1 Publication

Chemistry

DrugBankiDB01327. Cefazolin.
DB01413. Cefepime.
DB00267. Cefmenoxime.
DB00274. Cefmetazole.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB01331. Cefoxitin.
DB00430. Cefpiramide.
DB01416. Cefpodoxime.
DB00438. Ceftazidime.
DB01415. Ceftibuten.
DB01332. Ceftizoxime.
DB00303. Ertapenem.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Peptidoglycan synthase FtsIPRO_0000017052Add
BLAST
Propeptidei578 – 58811PRO_0000017053Add
BLAST

Proteomic databases

PaxDbiP0AD68.
PRIDEiP0AD68.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
divIBQ8DQM03EBI-548564,EBI-6446264From a different organism.
ftsLP0AEN44EBI-548564,EBI-1119082
ftsNP291313EBI-548564,EBI-1134233
ftsQP061365EBI-548564,EBI-1130157
ftsWP0ABG47EBI-548564,EBI-1214767
mtgAP460223EBI-548564,EBI-558469
ymgFP580343EBI-548564,EBI-1214577

Protein-protein interaction databases

DIPiDIP-47950N.
IntActiP0AD68. 18 interactions.
MINTiMINT-1031950.
STRINGi511145.b0084.

Structurei

3D structure databases

ProteinModelPortaliP0AD68.
SMRiP0AD68. Positions 71-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a C-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).

Sequence similaritiesi

Belongs to the transpeptidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0768.
HOGENOMiHOG000049554.
InParanoidiP0AD68.
KOiK03587.
OMAiNSFLKWR.
OrthoDBiEOG6N0HHV.
PhylomeDBiP0AD68.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AD68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP
60 70 80 90 100
DMLVKEGDMR SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD
110 120 130 140 150
AGGISVGDRW KALANALNIP LDQLSARINA NPKGRFIYLA RQVNPDMADY
160 170 180 190 200
IKKLKLPGIH LREESRRYYP SGEVTAHLIG FTNVDSQGIE GVEKSFDKWL
210 220 230 240 250
TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL QALVYRELNN
260 270 280 290 300
AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT
310 320 330 340 350
DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL
360 370 380 390 400
TLTGVLQKSS NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL
410 420 430 440 450
YPQKQRWSDI ERATFSFGYG LMVTPLQLAR VYATIGSYGI YRPLSITKVD
460 470 480 490 500
PPVPGERVFP ESIVRTVVHM MESVALPGGG GVKAAIKGYR IAIKTGTAKK
510 520 530 540 550
VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY YGGAVSAPVF
560 570 580
GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS
Length:588
Mass (Da):63,877
Last modified:March 20, 1987 - v1
Checksum:iC89A403D5980B2CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00137 Genomic DNA. Translation: AAA24300.1.
X55034 Genomic DNA. Translation: CAA38861.1.
U00096 Genomic DNA. Translation: AAC73195.1.
AP009048 Genomic DNA. Translation: BAB96652.1.
S49802 Genomic DNA. Translation: AAB24312.1.
S49875 Genomic DNA. Translation: AAB24310.1.
X55814 Genomic DNA. Translation: CAA39333.1.
PIRiA93123. ZPECP3.
RefSeqiNP_414626.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73195; AAC73195; b0084.
BAB96652; BAB96652; BAB96652.
GeneIDi944799.
KEGGiecj:Y75_p0083.
eco:b0084.
PATRICi32115273. VBIEscCol129921_0088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00137 Genomic DNA. Translation: AAA24300.1.
X55034 Genomic DNA. Translation: CAA38861.1.
U00096 Genomic DNA. Translation: AAC73195.1.
AP009048 Genomic DNA. Translation: BAB96652.1.
S49802 Genomic DNA. Translation: AAB24312.1.
S49875 Genomic DNA. Translation: AAB24310.1.
X55814 Genomic DNA. Translation: CAA39333.1.
PIRiA93123. ZPECP3.
RefSeqiNP_414626.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP0AD68.
SMRiP0AD68. Positions 71-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47950N.
IntActiP0AD68. 18 interactions.
MINTiMINT-1031950.
STRINGi511145.b0084.

Chemistry

ChEMBLiCHEMBL2354204.
DrugBankiDB01327. Cefazolin.
DB01413. Cefepime.
DB00267. Cefmenoxime.
DB00274. Cefmetazole.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB01331. Cefoxitin.
DB00430. Cefpiramide.
DB01416. Cefpodoxime.
DB00438. Ceftazidime.
DB01415. Ceftibuten.
DB01332. Ceftizoxime.
DB00303. Ertapenem.

Proteomic databases

PaxDbiP0AD68.
PRIDEiP0AD68.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73195; AAC73195; b0084.
BAB96652; BAB96652; BAB96652.
GeneIDi944799.
KEGGiecj:Y75_p0083.
eco:b0084.
PATRICi32115273. VBIEscCol129921_0088.

Organism-specific databases

EchoBASEiEB0337.
EcoGeneiEG10341. ftsI.

Phylogenomic databases

eggNOGiCOG0768.
HOGENOMiHOG000049554.
InParanoidiP0AD68.
KOiK03587.
OMAiNSFLKWR.
OrthoDBiEOG6N0HHV.
PhylomeDBiP0AD68.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:EG10341-MONOMER.
ECOL316407:JW0082-MONOMER.
MetaCyc:EG10341-MONOMER.

Miscellaneous databases

PROiP0AD68.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3."
    Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y.
    Mol. Gen. Genet. 191:1-9(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli mraR gene involved in cell growth and division."
    Ueki M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.
    J. Bacteriol. 174:7841-7843(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
    Strain: JE1011.
  6. "FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli."
    Guzman L.-M., Barondess J.J., Beckwith J.
    J. Bacteriol. 174:7716-7728(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
  7. "Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli."
    Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J.
    Biochem. J. 269:277-278(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-588.
  8. "Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site."
    Houba-Herin N., Hara H., Inouye M., Hirota Y.
    Mol. Gen. Genet. 201:499-504(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-307.
  9. "Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli."
    Nagasawa H., Sakagami Y., Suzuki A., Suzuki H., Hara H., Hirota Y.
    J. Bacteriol. 171:5890-5893(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  10. "An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli."
    Taschner P.E.M., Ypenburg N., Spratt B.G., Woldringh C.L.
    J. Bacteriol. 170:4828-4837(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-361.
  11. "Membrane topology of penicillin-binding protein 3 of Escherichia coli."
    Bowler L.D., Spratt B.G.
    Mol. Microbiol. 3:1277-1286(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiFTSI_ECOLI
AccessioniPrimary (citable) accession number: P0AD68
Secondary accession number(s): P04286
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: June 24, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.