A0A0E2HCS5 · A0A0E2HCS5_9FIRM

Function

function

Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionpenicillin binding
Molecular Functionpeptidoglycan glycosyltransferase activity
Molecular Functionserine-type D-Ala-D-Ala carboxypeptidase activity
Biological Processpeptidoglycan biosynthetic process
Biological Processproteolysis
Biological Processresponse to antibiotic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Penicillin-binding protein 1A
  • EC number

Gene names

    • ORF names
      HMPREF1090_01754

Organism names

Accessions

  • Primary accession
    A0A0E2HCS5

Proteomes

Subcellular Location

Cell membrane
; Single-pass type II membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane26-53Helical

Keywords

  • Cellular component

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain86-269Glycosyl transferase family 51
Domain448-708Penicillin-binding protein transpeptidase
Compositional bias859-889Polar residues
Region859-897Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    897
  • Mass (Da)
    98,132
  • Last updated
    2015-05-27 v1
  • Checksum
    67DB3275F2E7EB73
MNYGKYEAERRLKSLHSKSGKYASRLLLNIFKALFVLFLFLAVVGASIGFGMVKGIIDNAPSVDILNIQPSRFATAVYDSAGNLTDTLVTSGSNREEATYEELPKDLVNAFVAIEDSRFWTHNGIDIRSIARAVKGIVSDDYAGGGSTITQQLIKNNVFSGGMESGWGARIERKLQEQYLAVQLEKNSGMSKEDTKKLIITNYLNTINLGNNTLGVKVAAKRYFNKDVSDLTLSECTVLASITKNPSRLNPISGRENNAERRRIVLQYMYEQDYITKAQQEEALADDVYDRIQNVDTATKGINSHYSYFTDELIEQVINALMEKLDYTESQASNLLYSGGLQIYTTQDPALQAIVDEEINNPDNYSVAKYSVEYRLSITHADGTTEHYSEENLRTFRKSVLGDSSFEGLYASKEAVQDDIDQYKAWLLKDGDEIIGERQNLILQPQASFVLLDQHTGEVKALCGGRGEKTASLTLNRASNVYRQPGSAFKVITAFAPALDACGATLGTVYYDAPYTIGNKTFRNWWNSGYGFTGYSSIRDGIIYSMNIVAVRCLMETVTPQLGVEYAENMGITSLTKDDLGAATALGGITKGVSNLELTTAYAAIANGGVYTKPRFFTKILDHNGKVLIDNEPETKQVLKDSTAFLLTDAMSESMKSNRKFTRPGVSINSTSTRAALTGMTAAGKSGTTTSNNDVWFVGYTPYYTAGIWGGCDNNQKLKHGGVNNGGTSFHKDIWRNIMNRVHEGMSDPGFAVPDSIETAEICRKSGKRAVSGVCNHDPRGNAVYTEYFAKGTAPTEVCDKHVEVTVCAESGMRPTPYCPTKTTRVCMTLPEGEEGATDDSVFAIPGYCTVHSDVSTIIPPNTNEPGNTGPTVTPIGPGYQTSPETTEGFGPGNRPY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias859-889Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGYR01000014
EMBL· GenBank· DDBJ
ENZ17454.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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