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P0AD68 (FTSI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan synthase FtsI

EC=2.4.1.129
Alternative name(s):
Penicillin-binding protein 3
Short name=PBP-3
Peptidoglycan glycosyltransferase 3
Gene names
Name:ftsI
Synonyms:pbpB
Ordered Locus Names:b0084, JW0082
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

(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

Cell wall biogenesis; peptidoglycan biosynthesis.

Subcellular location

Cell inner membrane; Single-pass membrane protein; Periplasmic side. Note: The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space, where it acts on murein.

Domain

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 similarities

Belongs to the transpeptidase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
Cell cycle
Cell division
Cell shape
Cell wall biogenesis/degradation
Peptidoglycan synthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki

   Cellular_componentcell division site

Inferred from direct assay PubMed 9603865. Source: EcoliWiki

integral component of plasma membrane

Inferred from direct assay PubMed 319999. Source: EcoliWiki

intrinsic component of plasma membrane

Inferred from direct assay PubMed 3881388. Source: EcoliWiki

   Molecular_functionpenicillin binding

Inferred from direct assay PubMed 1103132. Source: EcoliWiki

peptidoglycan glycosyltransferase activity

Inferred from direct assay PubMed 7030331. Source: EcoliWiki

protein binding

Inferred from physical interaction PubMed 15774864PubMed 17185541PubMed 17938168PubMed 18165305PubMed 18978050PubMed 20847002PubMed 22885295PubMed 24561554. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Peptidoglycan synthase FtsI
PRO_0000017052
Propeptide578 – 58811
PRO_0000017053

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Potential
Topological domain40 – 577538Periplasmic Potential

Sites

Active site3071Acyl-ester intermediate

Experimental info

Mutagenesis3071S → A or T: Unable to bind penicillin. Ref.8
Mutagenesis3071S → C: Still able to bind penicillin. Ref.8
Mutagenesis3611N → 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. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P0AD68 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: C89A403D5980B2CD

FASTA58863,877
        10         20         30         40         50         60 
MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP DMLVKEGDMR 

        70         80         90        100        110        120 
SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD AGGISVGDRW KALANALNIP 

       130        140        150        160        170        180 
LDQLSARINA NPKGRFIYLA RQVNPDMADY IKKLKLPGIH LREESRRYYP SGEVTAHLIG 

       190        200        210        220        230        240 
FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL 

       250        260        270        280        290        300 
QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT 

       310        320        330        340        350        360 
DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL TLTGVLQKSS 

       370        380        390        400        410        420 
NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL YPQKQRWSDI ERATFSFGYG 

       430        440        450        460        470        480 
LMVTPLQLAR VYATIGSYGI YRPLSITKVD PPVPGERVFP ESIVRTVVHM MESVALPGGG 

       490        500        510        520        530        540 
GVKAAIKGYR IAIKTGTAKK VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY 

       550        560        570        580 
YGGAVSAPVF GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRZPECP3. A93123.
RefSeqNP_414626.1. NC_000913.3.
YP_488389.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AD68.
SMRP0AD68. Positions 60-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47950N.
IntActP0AD68. 17 interactions.
MINTMINT-1031950.
STRING511145.b0084.

Chemistry

ChEMBLCHEMBL2354204.

Proteomic databases

PaxDbP0AD68.
PRIDEP0AD68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73195; AAC73195; b0084.
BAB96652; BAB96652; BAB96652.
GeneID12932643.
944799.
KEGGecj:Y75_p0083.
eco:b0084.
PATRIC32115273. VBIEscCol129921_0088.

Organism-specific databases

EchoBASEEB0337.
EcoGeneEG10341. ftsI.

Phylogenomic databases

eggNOGCOG0768.
HOGENOMHOG000049554.
KOK03587.
OMAHPRYFNF.
OrthoDBEOG6N0HHV.
PhylomeDBP0AD68.

Enzyme and pathway databases

BioCycEcoCyc:EG10341-MONOMER.
ECOL316407:JW0082-MONOMER.
MetaCyc:EG10341-MONOMER.
UniPathwayUPA00219.

Gene expression databases

GenevestigatorP0AD68.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
ProtoNetSearch...

Other

PROP0AD68.

Entry information

Entry nameFTSI_ECOLI
AccessionPrimary (citable) accession number: P0AD68
Secondary accession number(s): P04286
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene