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P02918 (PBPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penicillin-binding protein 1A

Short name=PBP-1a
Short name=PBP1a

Including the following 2 domains:

  1. Penicillin-insensitive transglycosylase
    EC=2.4.2.-
    Alternative name(s):
    Peptidoglycan TGase
  2. Penicillin-sensitive transpeptidase
    EC=3.4.-.-
    Alternative name(s):
    DD-transpeptidase
Gene names
Name:mrcA
Synonyms:ponA
Ordered Locus Names:b3396, JW3359
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length850 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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).

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Subcellular location

Cell inner membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

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

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

Sequence caution

The sequence AAA58193.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAntibiotic resistance
Cell shape
Cell wall biogenesis/degradation
Peptidoglycan synthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Hydrolase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of cytolysis

Inferred from genetic interaction PubMed 7027927. Source: EcoCyc

peptidoglycan biosynthetic process

Inferred from direct assay PubMed 16840781. Source: EcoCyc

proteolysis

Inferred from direct assay PubMed 16840781Ref.5. Source: GOC

regulation of cell shape

Inferred from genetic interaction PubMed 7007327PubMed 9324260. Source: EcoCyc

response to antibiotic

Inferred from mutant phenotype PubMed 330236. Source: EcoCyc

   Cellular_componentintegral component of plasma membrane

Inferred from direct assay PubMed 319999. Source: EcoliWiki

   Molecular_functionpenicillin binding

Inferred from direct assay PubMed 330236. Source: EcoCyc

peptidoglycan glycosyltransferase activity

Inferred from direct assay PubMed 16840781. Source: EcoCyc

protein binding

Inferred from physical interaction PubMed 21183073PubMed 21183074. Source: IntAct

serine-type D-Ala-D-Ala carboxypeptidase activity

Inferred from direct assay PubMed 16840781. Source: EcoCyc

transferase activity, transferring pentosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

lpoAP454644EBI-1126191,EBI-557795

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 850850Penicillin-binding protein 1A
PRO_0000083164

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 850824Periplasmic Potential
Region48 – 216169Transglycosylase
Region400 – 710311Transpeptidase

Sites

Active site861Proton donor; for transglycosylase activity Potential
Active site4651Acyl-ester intermediate; for transpeptidase activity

Sequences

Sequence LengthMass (Da)Tools
P02918 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0A54C6B28783E34B

FASTA85093,636
        10         20         30         40         50         60 
MKFVKYFLIL AVCCILLGAG SIYGLYRYIE PQLPDVATLK DVRLQIPMQI YSADGELIAQ 

        70         80         90        100        110        120 
YGEKRRIPVT LDQIPPEMVK AFIATEDSRF YEHHGVDPVG IFRAASVALF SGHASQGAST 

       130        140        150        160        170        180 
ITQQLARNFF LSPERTLMRK IKEVFLAIRI EQLLTKDEIL ELYLNKIYLG YRAYGVGAAA 

       190        200        210        220        230        240 
QVYFGKTVDQ LTLNEMAVIA GLPKAPSTFN PLYSMDRAVA RRNVVLSRML DEGYITQQQF 

       250        260        270        280        290        300 
DQTRTEAINA NYHAPEIAFS APYLSEMVRQ EMYNRYGESA YEDGYRIYTT ITRKVQQAAQ 

       310        320        330        340        350        360 
QAVRNNVLDY DMRHGYRGPA NVLWKVGESA WDNNKITDTL KALPTYGPLL PAAVTSANPQ 

       370        380        390        400        410        420 
QATAMLADGS TVALSMEGVR WARPYRSDTQ QGPTPRKVTD VLQTGQQIWV RQVGDAWWLA 

       430        440        450        460        470        480 
QVPEVNSALV SINPQNGAVM ALVGGFDFNQ SKFNRATQAL RQVGSNIKPF LYTAAMDKGL 

       490        500        510        520        530        540 
TLASMLNDVP ISRWDASAGS DWQPKNSPPQ YAGPIRLRQG LGQSKNVVMV RAMRAMGVDY 

       550        560        570        580        590        600 
AAEYLQRFGF PAQNIVHTES LALGSASFTP MQVARGYAVM ANGGFLVDPW FISKIENDQG 

       610        620        630        640        650        660 
GVIFEAKPKV ACPECDIPVI YGDTQKSNVL ENNDVEDVAI SREQQNVSVP MPQLEQANQA 

       670        680        690        700        710        720 
LVAKTGAQEY APHVINTPLA FLIKSALNTN IFGEPGWQGT GWRAGRDLQR RDIGGKTGTT 

       730        740        750        760        770        780 
NSSKDAWFSG YGPGVVTSVW IGFDDHRRNL GHTTASGAIK DQISGYEGGA KSAQPAWDAY 

       790        800        810        820        830        840 
MKAVLEGVPE QPLTPPPGIV TVNIDRSTGQ LANGGNSREE YFIEGTQPTQ QAVHEVGTTI 

       850 
IDNGEAQELF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12."
Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.
Eur. J. Biochem. 147:437-446(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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.
[4]"Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12."
Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.
Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 452-480.
Strain: K12.
[5]"Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A."
Ishino F., Mitsui K., Tamaki S., Matsuhashi M.
Biochem. Biophys. Res. Commun. 97:287-293(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.
[6]"Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs."
Goffin C., Ghuysen J.-M.
Microbiol. Mol. Biol. Rev. 62:1079-1093(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02164 Genomic DNA. Translation: CAA26100.1.
U18997 Genomic DNA. Translation: AAA58193.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76421.2.
AP009048 Genomic DNA. Translation: BAE77895.1.
PIRZPECPA. G65134.
RefSeqNP_417855.4. NC_000913.3.
YP_492036.1. NC_007779.1.

3D structure databases

ProteinModelPortalP02918.
SMRP02918. Positions 47-789.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10251N.
IntActP02918. 8 interactions.
STRING511145.b3396.

Chemistry

ChEMBLCHEMBL2354204.
DrugBankDB01413. Cefepime.
DB00303. Ertapenem.

Protein family/group databases

CAZyGT51. Glycosyltransferase Family 51.

Proteomic databases

PaxDbP02918.
PRIDEP02918.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76421; AAC76421; b3396.
BAE77895; BAE77895; BAE77895.
GeneID12933998.
947907.
KEGGecj:Y75_p3780.
eco:b3396.
PATRIC32122224. VBIEscCol129921_3489.

Organism-specific databases

EchoBASEEB0741.
EcoGeneEG10748. mrcA.

Phylogenomic databases

eggNOGCOG5009.
HOGENOMHOG000041138.
KOK05366.
OMAMEIATGW.
OrthoDBEOG6HMXCD.
PhylomeDBP02918.

Enzyme and pathway databases

BioCycEcoCyc:EG10748-MONOMER.
ECOL316407:JW3359-MONOMER.
MetaCyc:EG10748-MONOMER.
UniPathwayUPA00219.

Gene expression databases

GenevestigatorP02918.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.710.10. 3 hits.
InterProIPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR012340. NA-bd_OB-fold.
IPR011816. PBP_1a.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamPF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
SSF56601. SSF56601. 4 hits.
TIGRFAMsTIGR02074. PBP_1a_fam. 1 hit.
ProtoNetSearch...

Other

PROP02918.

Entry information

Entry namePBPA_ECOLI
AccessionPrimary (citable) accession number: P02918
Secondary accession number(s): P76688, Q2M761
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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