P0AD68 · FTSI_ECOLI
- ProteinPeptidoglycan D,D-transpeptidase FtsI
- GeneftsI
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids588 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Required for localization of FtsN (PubMed:9282742).
Catalytic activity
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 307 | Acyl-ester intermediate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell division site | |
Cellular Component | divisome complex | |
Cellular Component | plasma membrane | |
Molecular Function | penicillin binding | |
Molecular Function | peptidoglycan glycosyltransferase activity | |
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | cell division | |
Biological Process | cell wall organization | |
Biological Process | division septum assembly | |
Biological Process | FtsZ-dependent cytokinesis | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | proteolysis | |
Biological Process | regulation of cell shape | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePeptidoglycan D,D-transpeptidase FtsI
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AD68
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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).
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 1-18 | Cytoplasmic | |||
Transmembrane | 19-39 | Helical | |||
Topological domain | 40-577 | Periplasmic | |||
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 23 | Impairs septal localization. | |||
Mutagenesis | 39 | Impairs septal localization. | |||
Mutagenesis | 46 | Impairs septal localization. | |||
Mutagenesis | 57 | Impairs recruitment of FtsN to the septal ring. | |||
Mutagenesis | 61 | Impairs recruitment of FtsN to the septal ring. | |||
Mutagenesis | 62 | Impairs recruitment of FtsN to the septal ring. | |||
Mutagenesis | 210 | Impairs recruitment of FtsN to the septal ring. | |||
Mutagenesis | 307 | Unable to bind penicillin. | |||
Mutagenesis | 307 | Still able to bind penicillin. | |||
Mutagenesis | 361 | In PBPBR1; obtained after selection for increased resistance to cephalexin, causes a change in the shape of the cell: The polar caps are pointed. | |||
Chemistry
Interaction
Subunit
Homodimer (PubMed:20847002).
Forms a complex with FtsW (PubMed:20847002).
Interacts with FtsQ (PubMed:17185541).
Forms a complex with FtsW (PubMed:20847002).
Interacts with FtsQ (PubMed:17185541).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
XENO | P0AD68 | divIB Q8DQM0 | 3 | EBI-548564, EBI-6446264 | |
BINARY | P0AD68 | ftsL P0AEN4 | 4 | EBI-548564, EBI-1119082 | |
BINARY | P0AD68 | ftsN P29131 | 3 | EBI-548564, EBI-1134233 | |
BINARY | P0AD68 | ftsQ P06136 | 5 | EBI-548564, EBI-1130157 | |
BINARY | P0AD68 | ftsW P0ABG4 | 7 | EBI-548564, EBI-1214767 | |
BINARY | P0AD68 | mrcB P02919 | 3 | EBI-548564, EBI-909769 | |
BINARY | P0AD68 | mtgA P46022 | 3 | EBI-548564, EBI-558469 | |
BINARY | P0AD68 | ymgF P58034 | 3 | EBI-548564, EBI-1214577 |
Complex viewer
Protein-protein interaction databases
Structure
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length588
- Mass (Da)63,877
- Last updated1987-03-20 v1
- ChecksumC89A403D5980B2CD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |