O70038 (O70038_STRPN) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 61.
History...
Names and origin
| Protein names | Submitted name: Penicillin-binding protein 1B EMBL BAD00805.1 Submitted name: Penicillin-binding protein 1b EMBL CAA05302.1 | ||
| Gene names |
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| Organism | Streptococcus pneumoniae EMBL CAA05302.1 | ||
| Taxonomic identifier | 1313 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 821 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation SAAS SAAS001264 Peptidoglycan synthesis SAAS SAAS001264 |
| Technical term | 3D-structure PDB 2JE5 PDB 2BG1 PDB 2JCH PDB 2FFF |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peptidoglycan-based cell wall Inferred from electronic annotation. Source: InterPro |
| Molecular function | catalytic activity Inferred from electronic annotation. Source: InterPro penicillin bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Complete sequences of six penicillin-binding protein genes from 40 Streptococcus pneumoniae clinical isolates collected in Japan." Sanbongi Y., Ida T., Ishikawa M., Osaki Y., Kataoka H., Suzuki T., Kondo K., Ohsawa F., Yonezawa M. Antimicrob. Agents Chemother. 48:2244-2250(2004) [PubMed: 15155228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: SP00077 EMBL BAD00805.1 and SP00079 EMBL BAD00807.1. |
| [2] | "Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae." Hakenbeck R., Konig A., Kern I., van der Linden M., Keck W., Billot-Klein D., Legrand R., Schoot B., Gutmann L. J. Bacteriol. 180:1831-1840(1998) [PubMed: 9537382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: R6 EMBL CAA05302.1. |
| [3] | "Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae." Hoskins J., Matsushima P., Mullen D.L., Tang J., Zhao G., Meier T.I., Nicas T.I., Jaskunas S.R. J. Bacteriol. 181:6552-6555(1999) [PubMed: 10515951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: R6 EMBL AAF04736.1. |
| [4] | "Active site restructuring regulates ligand recognition in class A penicillin-binding proteins." Macheboeuf P., Di Guilmi A.M., Job V., Vernet T., Dideberg O., Dessen A. Proc. Natl. Acad. Sci. U.S.A. 102:577-582(2005) [PubMed: 15637155] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 101-791. |
| [5] | "Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae." Lovering A.L., De Castro L., Lim D., Strynadka N.C. Protein Sci. 15:1701-1709(2006) [PubMed: 16751607] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 337-789. |
| [6] | "Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins." Macheboeuf P., Fischer D.S., Brown T., Zervosen A., Luxen A., Joris B., Dessen A., Schofield C.J. Nat. Chem. Biol. 3:565-569(2007) [PubMed: 17676039] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 74-791. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
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| EMBL GenBank DDBJ | AF101781 Genomic DNA. Translation: AAF04736.1. AB119817 Genomic DNA. Translation: BAD00805.1. AB119819 Genomic DNA. Translation: BAD00807.1. AJ002291 Genomic DNA. Translation: CAA05302.1. | ||||||||||||||||||||||||||||||
| PIR | B99110. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | O70038. | ||||||||||||||||||||||||||||||
| SMR | O70038. Positions 337-789. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||
| CAZy | GT51. Glycosyltransferase Family 51. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR012338. Beta-lactam/transpept-like. IPR001264. Glyco_trans_51. IPR001460. PCN-bd_Tpept. [Graphical view] | ||||||||||||||||||||||||||||||
| Gene3D | G3DSA:3.40.710.10. G3DSA:3.40.710.10. 1 hit. | ||||||||||||||||||||||||||||||
| Pfam | PF00912. Transgly. 1 hit. PF00905. Transpeptidase. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF56601. PBP_transp_fold. 1 hit. | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | O70038_STRPN | ||||||||
| Accession | Primary (citable) accession number: O70038 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
