Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Lantibiotic paenibacillin  

UniProtKB / Swiss-Prot ID :  LANPA_PAEPO

Gene Name (Synonyms) :  -
 

Species :  Paenibacillus polymyxa (Bacillus polymyxa). 

Subcellular Localization :  Secreted. 

Protein Function :  Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacks antibacterial activity against Gram- negative bacteria. 

Protein Sequence ASIIKTTIKVSKAVCKTLTCICTGSCSNCK...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylalanine.----ASIIK
----
22.27UniProtKB
Link-
22,3-didehydroalanine (Ser).---ASIIKT
---
36.38UniProtKB
Link-
62,3-didehydrobutyrine.SIIKTTIKV
24.28UniProtKB
Link-
72,3-didehydrobutyrine.IIKTTIKVS
17.50UniProtKB
Link-
11Lanthionine (Ser-Cys).TIKVSKAVC
15.19UniProtKB
Link-
17Beta-methyllanthionine (Thr-Cys).AVCKTLTCI
23.36UniProtKB
Link-
19Beta-methyllanthionine (Thr-Cys).CKTLTCICT
12.69UniProtKB
Link-
23Beta-methyllanthionine (Thr-Cys).TCICTGSCS
16.53UniProtKB
Link-
25Lanthionine (Ser-Cys).ICTGSCSNC
9.02UniProtKB
Link-
272,3-didehydroalanine (Ser).TGSCSNCK
47.13UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"N-terminal acetylation in paenibacillin, a novel lantibiotic.";
He Z., Yuan C., Zhang L., Yousef A.E.;
FEBS Lett. 582:2787-2792(2008).
Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, STRUCTURE BY NMR, ANDPOST-TRANSLATIONAL MODIFICATION.
Dehydroxylation
ReferencePubMed
"N-terminal acetylation in paenibacillin, a novel lantibiotic.";
He Z., Yuan C., Zhang L., Yousef A.E.;
FEBS Lett. 582:2787-2792(2008).
Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, STRUCTURE BY NMR, ANDPOST-TRANSLATIONAL MODIFICATION.
Thioether bond
ReferencePubMed
"N-terminal acetylation in paenibacillin, a novel lantibiotic.";
He Z., Yuan C., Zhang L., Yousef A.E.;
FEBS Lett. 582:2787-2792(2008).
Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, STRUCTURE BY NMR, ANDPOST-TRANSLATIONAL MODIFICATION.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures