Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Microcin C7  

UniProtKB / Swiss-Prot ID :  MCCC7_ECOLX

Gene Name (Synonyms) : 
mccA  

Species :  Escherichia coli. 

Subcellular Localization :   

Protein Function :  Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp. 

Protein Sequence MRTGNAN...
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-formylmethionine.----MRTGN
----
8.58UniProtKB
Link
7Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide.TGNAN
57.32UniProtKB
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
Formylation
ReferencePubMed
"Structure of microcin C51, a new antibiotic with a broad spectrum ofactivity.";
Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A.,Egorov T.A., Khmel I.A.;
FEBS Lett. 357:235-238(1995).
Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, FORMYLATION AT MET-1, ANDASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDE FORMATIONAT ASN-7.
"Chemical structure and translation inhibition studies of theantibiotic microcin C7.";
Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L.,Castilla M.A., Rico M., Moreno F., Delepierre M.;
J. Biol. Chem. 270:23520-23532(1995).
Cited for: STRUCTURE BY NMR, FUNCTION, MASS SPECTROMETRY, FORMYLATION AT MET-1,AND ASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDEFORMATION AT ASN-7.
Phosphorylation
ReferencePubMed
"Structure of microcin C51, a new antibiotic with a broad spectrum ofactivity.";
Metlitskaya A.Z., Katrukha G.S., Shashkov A.S., Zaitsev D.A.,Egorov T.A., Khmel I.A.;
FEBS Lett. 357:235-238(1995).
Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, FORMYLATION AT MET-1, ANDASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDE FORMATIONAT ASN-7.
"Chemical structure and translation inhibition studies of theantibiotic microcin C7.";
Guijarro J.I., Gonzalez-Pastor J.E., Baleux F., San Millan J.L.,Castilla M.A., Rico M., Moreno F., Delepierre M.;
J. Biol. Chem. 270:23520-23532(1995).
Cited for: STRUCTURE BY NMR, FUNCTION, MASS SPECTROMETRY, FORMYLATION AT MET-1,AND ASPARTIC ACID 1-[(3-AMINOPROPYL)(5'-ADENOSYL)PHOSPHONO]AMIDEFORMATION AT ASN-7.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures