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Searching in 'World-2DPAGE Repository [0022]' for entry matching: PBP_STAAU




World-2DPAGE Repository (0022):  PBP_STAAU

PBP_STAAU


General information about the entry
View entry in simple text format
Entry namePBP_STAAU
Primary accession numberP07944
integrated into World-2DPAGE Repository (0022) on May 7, 2010 (release 1)
2D Annotations were last modified onJune 22, 2011 (version 2)
General Annotations were last modified on November 24, 2011 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Beta-lactam-inducible penicillin-binding protein;.
Gene nameName=pbp
Annotated speciesRattus [TaxID: 10114]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae.
References
[1]   2D-PAGE GEL CHARACTERIZATION
DOI=10.1002/pmic.201000593;
Burniston J.G., Kenyani J., Wastling J.M., Burant C.F., Qi N.R., Koch L.G., Britton S.L.
''Proteomic analysis reveals perturbed energy metabolism and elevated oxidative stress in hearts of rats with inborn low aerobic capacity''
Proteomics 11(16):3369-3379 (2011)
2D PAGE maps for identified proteins
How to interpret a protein

HCR_LCR_HEART {HCR LCR Cardiac Map}
Rattus
Tissue: Heart
HCR_LCR_HEART
  map experimental info 		 
HCR_LCR_HEART

MAP LOCATIONS:
pI=6.26; Mw=36230  [identification data]

IDENTIFICATION: SPOT 178: SeqCov=33.5%. Peptides MS=12/20. Mascot PMF Score=106 [1].
PEPTIDE EVIDENCE: SPOT 178: 307-HKDYPFHAEV-316 (78) / 156-AIGVSNFNPLQIER-169 (105) / 178-YKPAVNQIECHPYLTQEK-195 (47) [1].
MAPPING (identification):
SPOT 178: Peptide mass fingerprinting [1]; Tandem mass spectrometry [1].

Copyright
Data from Dr. Jatin Burniston, Liverpool John Moores University, UK
Cross-references
UniProtKB/Swiss-ProtP07944; PBP_STAAU.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_11
Entry namePBP_STAAU
Primary accession numberP07944
Sequence was last modified on August 1, 1988 (version 1)
Annotations were last modified on April 5, 2011 (version 62)
Name and origin of the protein
DescriptionRecName: Full=Beta-lactam-inducible penicillin-binding protein;
Gene nameName=pbp
Encoded onName=pbp
KeywordsAntibiotic resistance; Cell cycle; Cell division; Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane; Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLY00688; CAA68684.1; -; Genomic_DNA
ProteinModelPortalP07944; -; .
SMRP07944; 27-670; .
GOGO:0016021; C:integral to membrane; IEA:UniProtKB-KW; .
GOGO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell; .
GOGO:0008658; F:penicillin binding; IEA:InterPro; .
GOGO:0007049; P:cell cycle; IEA:UniProtKB-KW; .
GOGO:0051301; P:cell division; IEA:UniProtKB-KW; .
GOGO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW; .
GOGO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW; .
GOGO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW; .
GOGO:0046677; P:response to antibiotic; IEA:UniProtKB-KW; .
InterProIPR012338; Beta-lactam/transpept-like; .
InterProIPR007887; MecA_N; .
InterProIPR005311; PBP_dimer; .
InterProIPR001460; PCN-bd_Tpept; .
Gene3DG3DSA:3.40.710.10; G3DSA:3.40.710.10; 1; .
PfamPF05223; MecA_N; 1; .
PfamPF03717; PBP_dimer; 1; .
PfamPF00905; Transpeptidase; 1; .
SUPFAMSSF56519; PBP_dimer; 1; .
SUPFAMSSF56601; PBP_transp_fold; 1; .


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