pbpC:Gene Product(s)
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Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
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Standard name |
PbpC |
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Synonyms |
fused transglycosylase[1], transpeptidase[1], B2519[2][1], YfgN[2][1], PbpC[2][1], PBP1C[2][1] , ECK2515, JW2503, yfgN, b2519 |
Product description |
putative peptidoglycan enzyme[2][3] Penicillin-binding protein PBP1C murein transglycosylase[4] |
EC number (for enzymes) | |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0030288 |
outer membrane-bounded periplasmic space |
C |
Seeded from Riley et al 2006 [1]. |
Missing: evidence, reference | ||||
GO:0005886 |
plasma membrane |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005886 |
plasma membrane |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0008360 |
regulation of cell shape |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0008658 |
penicillin binding |
IDA: Inferred from Direct Assay |
F |
Table 3 shows ampicillin inhibiting cell division when binding to PBP 3. |
complete | |||
GO:0009252 |
peptidoglycan biosynthetic process |
IDA: Inferred from Direct Assay |
P |
Figure 2 shows formation of peptidoglycan when placed in a solution with penicillin binding protein 3. |
complete | |||
GO:0009252 |
peptidoglycan biosynthetic process |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009274 |
peptidoglycan-based cell wall |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016020 |
membrane |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016021 |
integral to membrane |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016021 |
integral to membrane |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-9906 |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0051781 |
positive regulation of cell division |
IDA: Inferred from Direct Assay |
P |
Table 3 shows inhibition of cell division when penicillin binding protein 3 is competing with ampicillin. |
complete | |||
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
lon |
Experiment(s):EBI-1143101 | ||
Protein |
htpG |
Experiment(s):EBI-1143101 | ||
Protein |
rplB |
Experiment(s):EBI-1143101 | ||
Protein |
maeB |
Experiment(s):EBI-1143101 | ||
Protein |
groL |
Experiment(s):EBI-1143101 | ||
Protein |
rpsE |
Experiment(s):EBI-1143101 | ||
Protein |
clpB |
Experiment(s):EBI-1143101 | ||
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
Inner membrane |
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membrane |
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MPRLLTKRGC WITLAAAPFL LFLAAWGADK LWPLPLHEVN PARVVVAQDG TPLWRFADAD GIWRYPVTIE DVSPRYLEAL INYEDRWFWK HPGVNPFSVA RAAWQDLTSG RVISGGSTLT MQVARLLDPH PKTFGGKIRQ LWRALQLEWH LSKREILTLY LNRAPFGGTL QGIGAASWAY LGKSPANLSY SEAAMLAVLP QAPSRLRPDR WPERAEAARN KVLERMAVQG VWSREQVKES REEPIWLAPR QMPQLAPLFS RMMLGKSKSD KITTTLDAGL QRRLEELAQN WKGRLPPRSS LAMIVVDHTD MRVRGWVGSV DLNDDSRFGH VDMVNSIRSP GSVLKPFVYG LALDEGLIHP ASLLQDVPRR TGDYRPGNFD SGFHGPISMS EALVRSLNLP AVQVLEAYGP KRFAAKLRNV GLPLYLPNGA APNLSLILGG AGAKLEDMAA AYTAFARHGK AGKLRLQPDD PLLERPLMSS GAAWIIRRIM ADEAQPLPDS ALPRVAPLAW KTGTSYGYRD AWAIGVNARY VIGIWTGRPD GTPVVGQFGF ASAVPLLNQV NNILLSRSAN LPEDPRPNSV TRGVICWPGG QSLPEGDGNC RRRLATWLLD GSQPPTLLLP EQEGINGIRF PIWLDENGKR VAADCPQARQ EMINVWPLPL EPWLPASERR AVRLPPASTS CPPYGHDAQL PLQLTGVRDG AIIKRLPGAA EATLPLQSSG GAGERWWFLN GEPLTERGRN VTLHLTDKGD YQLLVMDDVG QIATVKFVMQ |
Length |
770 |
Mol. Wt |
85.068 kDa |
pI |
9.9 (calculated) |
Extinction coefficient |
172,340 - 172,965 (calc based on 16 Y, 27 W, and 5 C residues) |
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Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
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Resource type | Source | Notes/Reference |
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 Spratt, BG (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 72 2999-3003 PubMed
- ↑ Ishino, F & Matsuhashi, M (1981) Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence. Biochem. Biophys. Res. Commun. 101 905-11 PubMed
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
- ↑ Schiffer, G & Höltje, JV (1999) Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli. J. Biol. Chem. 274 32031-9 PubMed
- ↑ 9.0 9.1 9.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
Categories
- GO:0030288 ! outer membrane-bounded periplasmic space
- GO:0005886 ! plasma membrane
- GO:0008360 ! regulation of cell shape
- GO:0008658 ! penicillin binding
- GO:0009252 ! peptidoglycan biosynthetic process
- GO:0009274 ! peptidoglycan-based cell wall
- GO:0016020 ! membrane
- GO:0016021 ! integral component of membrane
- GO:0051781 ! positive regulation of cell division
- Proteins