P0AD68 · FTSI_ECOLI

Function

function

Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:3531167, PubMed:6450748, PubMed:7030331, PubMed:9614966).
Required for localization of FtsN (PubMed:9282742).

Caution

Was originally thought to be a bifunctional enzyme with transglycosylase and transpeptidase activities.

Catalytic activity

  • Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
    EC:3.4.16.4 (UniProtKB | ENZYME | Rhea)

Activity regulation

Inhibited by beta-lactam antibiotics such as penicillin, moenomycin, macarbomycin, furazlocillin and piperacillin. Antibiotics inhibit the activity by binding to the catalytic serine.

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site307Acyl-ester intermediate

GO annotations

AspectTerm
Cellular Componentcell division site
Cellular Componentdivisome complex
Cellular Componentplasma membrane
Molecular Functionpenicillin binding
Molecular Functionpeptidoglycan glycosyltransferase activity
Molecular Functionserine-type D-Ala-D-Ala carboxypeptidase activity
Biological Processcell division
Biological Processcell wall organization
Biological Processdivision septum assembly
Biological ProcessFtsZ-dependent cytokinesis
Biological Processpeptidoglycan biosynthetic process
Biological Processproteolysis
Biological Processregulation of cell shape
Biological Processresponse to xenobiotic stimulus

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidoglycan D,D-transpeptidase FtsI
  • EC number
  • Alternative names
    • Essential cell division protein FtsI
    • Murein transpeptidase
    • Penicillin-binding protein 3
      (PBP-3
      )
    • Peptidoglycan synthase FtsI

Gene names

    • Name
      ftsI
    • Synonyms
      pbpB
    • Ordered locus names
      b0084, JW0082

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • JE1011
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AD68
  • Secondary accessions
    • P04286

Proteomes

Subcellular Location

Cell inner membrane
; Single-pass membrane protein
Note: The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space (PubMed:2677607, PubMed:9614966).
Localizes to the division septum during the later stages of cell growth and throughout septation (PubMed:15601716, PubMed:9379897, PubMed:9603865, PubMed:9882665).
Localization is dependent on FtsZ, FtsA, FtsK, FtsQ, FtsL and FtsW, but not on FtsN (PubMed:11703663, PubMed:11807049, PubMed:9603865, PubMed:9882665).

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-18Cytoplasmic
Transmembrane19-39Helical
Topological domain40-577Periplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis23Impairs septal localization.
Mutagenesis39Impairs septal localization.
Mutagenesis46Impairs septal localization.
Mutagenesis57Impairs recruitment of FtsN to the septal ring.
Mutagenesis61Impairs recruitment of FtsN to the septal ring.
Mutagenesis62Impairs recruitment of FtsN to the septal ring.
Mutagenesis210Impairs recruitment of FtsN to the septal ring.
Mutagenesis307Unable to bind penicillin.
Mutagenesis307Still able to bind penicillin.
Mutagenesis361In PBPBR1; obtained after selection for increased resistance to cephalexin, causes a change in the shape of the cell: The polar caps are pointed.

Chemistry

PTM/Processing

Features

Showing features for chain, propeptide.

Type
IDPosition(s)Description
ChainPRO_00000170521-577Peptidoglycan D,D-transpeptidase FtsI
PropeptidePRO_0000017053578-588

Proteomic databases

Interaction

Subunit

Homodimer (PubMed:20847002).
Forms a complex with FtsW (PubMed:20847002).
Interacts with FtsQ (PubMed:17185541).

Binary interactions

Type
Entry 1Entry 2Number of experimentsIntAct
XENO P0AD68divIB Q8DQM03EBI-548564, EBI-6446264
BINARY P0AD68ftsL P0AEN44EBI-548564, EBI-1119082
BINARY P0AD68ftsN P291313EBI-548564, EBI-1134233
BINARY P0AD68ftsQ P061365EBI-548564, EBI-1130157
BINARY P0AD68ftsW P0ABG47EBI-548564, EBI-1214767
BINARY P0AD68mrcB P029193EBI-548564, EBI-909769
BINARY P0AD68mtgA P460223EBI-548564, EBI-558469
BINARY P0AD68ymgF P580343EBI-548564, EBI-1214577

Complex viewer

Protein-protein interaction databases

Family & Domains

Domain

Contains an N-terminal membrane anchor-containing module, a central non-catalytic domain and a C-terminal penicillin-binding (PB) catalytic domain. The transmembrane region is essential for localization to the septal ring, interaction with FtsW and cell septation.

Sequence similarities

Belongs to the transpeptidase family. FtsI subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    588
  • Mass (Da)
    63,877
  • Last updated
    1987-03-20 v1
  • Checksum
    C89A403D5980B2CD
MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
K00137
EMBL· GenBank· DDBJ
AAA24300.1
EMBL· GenBank· DDBJ
Genomic DNA
X55034
EMBL· GenBank· DDBJ
CAA38861.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC73195.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAB96652.1
EMBL· GenBank· DDBJ
Genomic DNA
S49802
EMBL· GenBank· DDBJ
AAB24312.1
EMBL· GenBank· DDBJ
Genomic DNA
S49875
EMBL· GenBank· DDBJ
AAB24310.1
EMBL· GenBank· DDBJ
Genomic DNA
X55814
EMBL· GenBank· DDBJ
CAA39333.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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