Penicillin-binding protein 2 - Escherichia coli (strain K12)

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P0AD65 (PBP2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Penicillin-binding protein 2
Short name=PBP-2

Gene names

Name:	mrdA
Synonyms:	pbpA
Ordered Locus Names:	b0635, JW0630

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Domain	Has a penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).
Sequence similarities	Belongs to the transpeptidase family.

Ontologies

Keywords
Biological process	Antibiotic resistance Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cell wall organization Inferred from mutant phenotype PubMed 11418550 PubMed 18390656 PubMed 3326629. Source: EcoCyc peptidoglycan biosynthetic process Inferred from mutant phenotype PubMed 18390656 PubMed 8760906. Source: EcoCyc regulation of cell shape Inferred from mutant phenotype PubMed 11418550 PubMed 12519203 PubMed 17513478 PubMed 18390656 PubMed 3894330. Source: EcoCyc response to antibiotic Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki response to drug Inferred from direct assay PubMed 17470659 PubMed 18250190 PubMed 18390656. Source: EcoCyc
Cellular_component	integral to plasma membrane Inferred from direct assay PubMed 1103132. Source: EcoliWiki
Molecular_function	penicillin binding Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki peptidoglycan L,D-transpeptidase activity Inferred from direct assay PubMed 6297485. Source: EcoliWiki serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from direct assay PubMed 3009484. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 633

633

Penicillin-binding protein 2

PRO_0000195444

Sites

Active site

330

Acyl-ester intermediate

Sequences

Sequence

Length

Mass (Da)

Tools

P0AD65 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: FE2305C002743AF6
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FASTA

633

70,857

        10         20         30         40         50         60 
MKLQNSFRDY TAESALFVRR ALVAFLGILL LTGVLIANLY NLQIVRFTDY QTRSNENRIK 

        70         80         90        100        110        120 
LVPIAPSRGI IYDRNGIPLA LNRTIYQIEM MPEKVDNVQQ TLDALRSVVD LTDDDIAAFR 

       130        140        150        160        170        180 
KERARSHRFT SIPVKTNLTE VQVARFAVNQ YRFPGVEVKG YKRRYYPYGS ALTHVIGYVS 

       190        200        210        220        230        240 
KINDKDVERL NNDGKLANYA ATHDIGKLGI ERYYEDVLHG QTGYEEVEVN NRGRVIRQLK 

       250        260        270        280        290        300 
EVPPQAGHDI YLTLDLKLQQ YIETLLAGSR AAVVVTDPRT GGVLALVSTP SYDPNLFVDG 

       310        320        330        340        350        360 
ISSKDYSALL NDPNTPLVNR ATQGVYPPAS TVKPYVAVSA LSAGVITRNT TLFDPGWWQL 

       370        380        390        400        410        420 
PGSEKRYRDW KKWGHGRLNV TRSLEESADT FFYQVAYDMG IDRLSEWMGK FGYGHYTGID 

       430        440        450        460        470        480 
LAEERSGNMP TREWKQKRFK KPWYQGDTIP VGIGQGYWTA TPIQMSKALM ILINDGIVKV 

       490        500        510        520        530        540 
PHLLMSTAED GKQVPWVQPH EPPVGDIHSG YWELAKDGMY GVANRPNGTA HKYFASAPYK 

       550        560        570        580        590        600 
IAAKSGTAQV FGLKANETYN AHKIAERLRD HKLMTAFAPY NNPQVAVAMI LENGGAGPAV 

       610        620        630 
GTLMRQILDH IMLGDNNTDL PAENPAVAAA EDH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12." Asoh S., Matsuzawa H., Ishino F., Strominger J.L., Matsuhashi M., Ohta T. Eur. J. Biochem. 160:231-238(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon." Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T. J. Bacteriol. 171:558-560(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 606-633. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04516 Genomic DNA. Translation: CAA28201.1. U82598 Genomic DNA. Translation: AAB40835.1. U00096 Genomic DNA. Translation: AAC73736.1. AP009048 Genomic DNA. Translation: BAA35282.1. M22857 Genomic DNA. Translation: AAA24570.1.
PIR	ZPECP2. C24995.
RefSeq	NP_415168.1. NC_000913.2. YP_488926.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AD65.
SMR	P0AD65. Positions 56-614.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48190N.
IntAct	P0AD65. 2 interactions.
STRING	511145.b0635.
Proteomic databases
PaxDb	P0AD65.
PRIDE	P0AD65.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73736; AAC73736; b0635. BAA35282; BAA35282; BAA35282.
GeneID	12930918. 945240.
KEGG	ecj:Y75_p0625. eco:b0635.
PATRIC	32116453. VBIEscCol129921_0666.
Organism-specific databases
EchoBASE	EB0601.
EcoGene	EG10606. mrdA.
Phylogenomic databases
eggNOG	COG0768.
HOGENOM	HOG000266120.
KO	K05515.
OMA	TKLIQTQ.
ProtClustDB	PRK10795.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10606-MONOMER. ECOL316407:JW0630-MONOMER. MetaCyc:EG10606-MONOMER.
UniPathway	UPA00219.
Gene expression databases
Genevestigator	P0AD65.
Family and domain databases
Gene3D	3.40.710.10. 1 hit.
InterPro	IPR012338. Beta-lactam/transpept-like. IPR005311. PBP_dimer. IPR001460. PCN-bd_Tpept. IPR017790. Penicillin-binding_protein_2. [Graphical view]
Pfam	PF03717. PBP_dimer. 1 hit. PF00905. Transpeptidase. 1 hit. [Graphical view]
SUPFAM	SSF56519. PBP_dimer. 1 hit. SSF56601. PBP_transp_fold. 1 hit.
TIGRFAMs	TIGR03423. pbp2_mrdA. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1840.

Entry information

Entry name

PBP2_ECOLI

Accession

Primary (citable) accession number: P0AD65
Secondary accession number(s): P08150

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents