P76577 · PBPC_ECOLI

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

Activity regulation

Transglycosylase activity can be inhibited by moenomycin.

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site84Proton donor; for transglycosylase activity
Active site342Acyl-ester intermediate; for transpeptidase activity

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functioncarboxypeptidase activity
Molecular Functionpenicillin binding
Molecular Functionpeptidoglycan glycosyltransferase activity
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processpositive regulation of cell division
Biological Processproteolysis
Biological Processregulation of cell shape
Biological Processresponse to antibiotic

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Penicillin-binding protein 1C
  • Short names
    PBP-1c; PBP1c

Including 2 domains:

  • Recommended name
    Penicillin-insensitive transglycosylase
  • EC number
  • Alternative names
    • Peptidoglycan TGase
  • Recommended name
    Transpeptidase-like module

Gene names

    • Name
      pbpC
    • Synonyms
      yfgN
    • Ordered locus names
      b2519, JW2503

Organism names

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

Accessions

  • Primary accession
    P76577
  • Secondary accessions
    • P76986
    • P76988

Proteomes

Subcellular Location

Cell inner membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-8Cytoplasmic
Transmembrane9-29Helical; Signal-anchor for type II membrane protein
Topological domain30-770Periplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Deletion results in an altered mode of murein synthesis.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000831881-770Penicillin-binding protein 1C

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region43-213Transglycosylase
Region278-559Transpeptidase

Sequence similarities

In the N-terminal section; belongs to the glycosyltransferase 51 family.
In the C-terminal section; belongs to the transpeptidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    770
  • Mass (Da)
    85,067
  • Last updated
    1997-02-01 v1
  • Checksum
    B227162E5381BEAD
MPRLLTKRGCWITLAAAPFLLFLAAWGADKLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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