P76577 · PBPC_ECOLI
- ProteinPenicillin-binding protein 1C
- GenepbpC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids770 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional.
Miscellaneous
Due to the fact that PBP-1c can neither substitute for PBP-1a or PBP-1b, nor rescue a PBP-1a/PBP-1b double mutant, it is possible that PBP-1c has its own distinct function. Moreover it does not bind to most of the beta-lactams known to bind to other binding proteins, suggesting that the penicillin-binding domain must be different from those present in PBP-1a and PBP-1b. It may function as a transglycosylase only.
Catalytic activity
- [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H+
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate RHEA-COMP:9602 + CHEBI:60033 = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate RHEA-COMP:9603 + CHEBI:58405 + CHEBI:15378
Activity regulation
Transglycosylase activity can be inhibited by moenomycin.
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 84 | Proton donor; for transglycosylase activity | ||||
Sequence: E | ||||||
Active site | 342 | Acyl-ester intermediate; for transpeptidase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | penicillin binding | |
Molecular Function | peptidoglycan glycosyltransferase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | positive regulation of cell division | |
Biological Process | proteolysis | |
Biological Process | regulation of cell shape | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1C
- Short namesPBP-1c; PBP1c
Including 2 domains:
- Recommended namePenicillin-insensitive transglycosylase
- EC number
- Alternative names
- Recommended nameTranspeptidase-like module
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP76577
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-8 | Cytoplasmic | ||||
Sequence: MPRLLTKR | ||||||
Transmembrane | 9-29 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: GCWITLAAAPFLLFLAAWGAD | ||||||
Topological domain | 30-770 | Periplasmic | ||||
Sequence: KLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ |
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083188 | 1-770 | Penicillin-binding protein 1C | |||
Sequence: MPRLLTKRGCWITLAAAPFLLFLAAWGADKLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ |
Proteomic databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 43-213 | Transglycosylase | ||||
Sequence: RVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPE | ||||||
Region | 278-559 | Transpeptidase | ||||
Sequence: AGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQ |
Sequence similarities
In the N-terminal section; belongs to the glycosyltransferase 51 family.
In the C-terminal section; belongs to the transpeptidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length770
- Mass (Da)85,067
- Last updated1997-02-01 v1
- ChecksumB227162E5381BEAD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U88571 EMBL· GenBank· DDBJ | AAB48052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75572.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16410.2 EMBL· GenBank· DDBJ | Genomic DNA |