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Protein

Penicillin-binding protein 2

Gene

mrdA

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. Its synthesize cross-linked peptidoglycan from the lipid intermediates (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei330 – 3301Acyl-ester intermediateBy similarity

GO - Molecular functioni

  1. catalytic activity Source: UniProtKB-KW
  2. penicillin binding Source: InterPro

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
  3. regulation of cell shape Source: UniProtKB-KW
  4. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciECOL199310:C0726-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 2
Short name:
PBP-2
Gene namesi
Name:mrdA
Synonyms:pbpA
Ordered Locus Names:c0726
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001410: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Penicillin-binding protein 2PRO_0000195446Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi199310.c0726.

Structurei

3D structure databases

ProteinModelPortaliP0AD66.
SMRiP0AD66. Positions 56-614.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Has a penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).By similarity

Sequence similaritiesi

Belongs to the transpeptidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000266120.
KOiK05515.
OMAiARNYSAY.
OrthoDBiEOG6N0HHV.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
IPR017790. Penicillin-binding_protein_2.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
TIGRFAMsiTIGR03423. pbp2_mrdA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AD66-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY
60 70 80 90 100
QTRSNENRIK LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ
110 120 130 140 150
TLDALRSVVD LTDDDIAAFR KERARSHRFT SIPVKTNLTE VQVARFAVNQ
160 170 180 190 200
YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS KINDKDVERL NNDGKLANYA
210 220 230 240 250
ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK EVPPQAGHDI
260 270 280 290 300
YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG
310 320 330 340 350
ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT
360 370 380 390 400
TLFDPGWWQL PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG
410 420 430 440 450
IDRLSEWMGK FGYGHYTGID LAEERSGNMP TREWKQKRFK KPWYQGDTIP
460 470 480 490 500
VGIGQGYWTA TPIQMSKALM ILINDGIVKV PHLLMSTAED GKQVPWVQPH
510 520 530 540 550
EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK IAAKSGTAQV
560 570 580 590 600
FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV
610 620 630
GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH
Length:633
Mass (Da):70,857
Last modified:August 1, 1988 - v1
Checksum:iFE2305C002743AF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN79199.1.
RefSeqiNP_752656.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN79199; AAN79199; c0726.
GeneIDi1037029.
KEGGiecc:c0726.
PATRICi18279491. VBIEscCol75197_0689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN79199.1.
RefSeqiNP_752656.1. NC_004431.1.

3D structure databases

ProteinModelPortaliP0AD66.
SMRiP0AD66. Positions 56-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c0726.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN79199; AAN79199; c0726.
GeneIDi1037029.
KEGGiecc:c0726.
PATRICi18279491. VBIEscCol75197_0689.

Phylogenomic databases

HOGENOMiHOG000266120.
KOiK05515.
OMAiARNYSAY.
OrthoDBiEOG6N0HHV.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciECOL199310:C0726-MONOMER.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
IPR017790. Penicillin-binding_protein_2.
[Graphical view]
PfamiPF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
TIGRFAMsiTIGR03423. pbp2_mrdA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CFT073 / ATCC 700928 / UPEC.

Entry informationi

Entry nameiPBP2_ECOL6
AccessioniPrimary (citable) accession number: P0AD66
Secondary accession number(s): P08150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.