Q1KLY5 · CAMP_CEBCA
- ProteinCathelicidin antimicrobial peptide
- GeneCAMP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids170 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Antimicrobial protein that is an integral component of the innate immune system (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (By similarity).
Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (By similarity).
The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (By similarity).
Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (By similarity).
The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (By similarity).
Antibacterial peptide LL-37
Antimicrobial peptide that is an integral component of the innate immune system (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Causes membrane permeabilization by forming transmembrane pores (in vitro) (By similarity).
Causes lysis of E.coli (By similarity).
Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram-positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (By similarity).
Exhibits antimicrobial activity against methicillin-resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (By similarity).
Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (By similarity).
May form supramolecular fiber-like assemblies on bacterial membranes (By similarity).
Induces cytokine and chemokine producation as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (By similarity).
Exhibits hemolytic activity against red blood cells (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Causes membrane permeabilization by forming transmembrane pores (in vitro) (By similarity).
Causes lysis of E.coli (By similarity).
Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram-positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (By similarity).
Exhibits antimicrobial activity against methicillin-resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (By similarity).
Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (By similarity).
May form supramolecular fiber-like assemblies on bacterial membranes (By similarity).
Induces cytokine and chemokine producation as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (By similarity).
Exhibits hemolytic activity against red blood cells (By similarity).
Antibacterial peptide FALL-39
Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | vesicle | |
Molecular Function | lipopolysaccharide binding | |
Biological Process | antimicrobial humoral immune response mediated by antimicrobial peptide | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | innate immune response | |
Biological Process | neutrophil activation |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCathelicidin antimicrobial peptide
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Cebidae > Cebinae > Cebus
Accessions
- Primary accessionQ1KLY5
PTM/Processing
Features
Showing features for signal, propeptide, disulfide bond, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MKTQRDGPSLGRWSLVLLLLGLTMPLAITA | ||||||
Propeptide | PRO_0000251746 | 31-131 | Cathelin-like domain (CLD) | |||
Sequence: QVLSYQEAVLRAVDGLNQRSLDANLYRLLNLDPRPTLDGDPDTPKPVSFTVKETVCPRTIQRSPEECDFKKDGLVKRCVGTVILNQARDSFDISCDKDERK | ||||||
Disulfide bond | 86↔97 | |||||
Sequence: CPRTIQRSPEEC | ||||||
Disulfide bond | 108↔125 | |||||
Sequence: CVGTVILNQARDSFDISC | ||||||
Peptide | PRO_0000251747 | 132-170 | Antibacterial peptide FALL-39 | |||
Sequence: VARLGGFLQKAREKIARGFKKIGQKINDFLGKLAPRTEA | ||||||
Peptide | PRO_0000251748 | 134-170 | Antibacterial peptide LL-37 | |||
Sequence: RLGGFLQKAREKIARGFKKIGQKINDFLGKLAPRTEA |
Post-translational modification
Proteolytically cleaved by proteinase PRTN3 into antibacterial peptide LL-37 (By similarity).
Proteolytically cleaved by cathepsin CTSG and neutrophil elastase ELANE (By similarity).
Proteolytically cleaved by cathepsin CTSG and neutrophil elastase ELANE (By similarity).
Antibacterial peptide LL-37
Resistant to proteolytic degradation in solution, and when bound to both zwitterionic (mimicking mammalian membranes) and negatively charged membranes (mimicking bacterial membranes).
After secretion onto the skin surface, the CAMP gene product is processed by a serine protease-dependent mechanism into multiple novel antimicrobial peptides distinct from and shorter than cathelicidin LL-37 (By similarity).
These peptides show enhanced antimicrobial action, acquiring the ability to kill skin pathogens such as S.aureus, E.coli and C.albicans. These peptides have lost the ability to stimulate CXCL8/IL8 release from keratinocytes (By similarity).
The peptides act synergistically, killing bacteria at lower concentrations when present together, and maintain activity at increased salt condition (By similarity).
These peptides show enhanced antimicrobial action, acquiring the ability to kill skin pathogens such as S.aureus, E.coli and C.albicans. These peptides have lost the ability to stimulate CXCL8/IL8 release from keratinocytes (By similarity).
The peptides act synergistically, killing bacteria at lower concentrations when present together, and maintain activity at increased salt condition (By similarity).
Keywords
- PTM
Interaction
Subunit
Antibacterial peptide LL-37
Monomer, homodimer or homotrimer (in vitro) (By similarity).
Oligomerizes as tetra- or hexamer in solution (in vitro) (By similarity).
Oligomerizes as tetra- or hexamer in solution (in vitro) (By similarity).
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 150-162 | Active core | ||||
Sequence: FKKIGQKINDFLG |
Domain
The cathelin-like domain (CLD), which is the propeptide part, does not seem to exhibit auto-inhibitory function, as it does not inhibit the antibacterial activity of antibacterial peptide LL-37.
Antibacterial peptide LL-37
Undergoes conformational change in the presence of lipid A, transitioning from a random coil to an alpha-helical structure.
Antibacterial peptide LL-37
Residues 17-29 of LL-37 represent the active core of the antimicrobial peptide. Forms ribbon-like fibrils and exhibits antibacterial activity against Gram-positive M.luteus (By similarity).
Also exhibits antibacterial activity against Gram-negative E.coli and P.fluorescens (By similarity).
Also exhibits antibacterial activity against Gram-negative E.coli and P.fluorescens (By similarity).
Sequence similarities
Belongs to the cathelicidin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length170
- Mass (Da)18,967
- Last updated2006-05-30 v1
- Checksum5830E3F24647DEA7