Bacteriocin: Colicin-M
Accession: BAC135
Classification
Class: Unclassified
Genetics
Gene: cma
Producer and target organisms
Producer Organism: Escherichia coli [Gram-negative]
Taxonomy: Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacteriales
Enterobacteriaceae
Escherichia
Target organismsEnterobacteriaceae - Escherichia coli
Description
colicin M contains a pentapeptide (Glu-Thr-Leu-Thr-Val) in the domain required for uptake into cells.
A similar sequence was found in all colicins which are taken up by a TonB-dependent mechanism and in outer membrane receptor proteins which are constituents of TonB-dependent transport systems.
The structure of colicin M in the carboxy-terminal activity domain had no resemblance to the pore-forming colicins or colicins with endonuclease activity.
A similar sequence was found in all colicins which are taken up by a TonB-dependent mechanism and in outer membrane receptor proteins which are constituents of TonB-dependent transport systems.
The structure of colicin M in the carboxy-terminal activity domain had no resemblance to the pore-forming colicins or colicins with endonuclease activity.
Uniprot and PDB links
UniProt Entry: P05820
PDB Entry2XMX resolved by X-RAY 2XTQ resolved by X-RAY 2XTR resolved by X-RAY 3DA3 resolved by X-RAY 3DA4 resolved by X-RAY
NUCLEOTIDE SEQUENCE, [GENOMIC DNA].
MEDLINE=87250310;PubMed=3036784;
RA Koeck J., Oelschlaeger T., Kamp R.M., Braun V.
"Primary structure of colicin M, an inhibitor of murein biosynthesis.", J. Bacteriol. 169:3358-3361(1987).
MEDLINE=87250310;PubMed=3036784;
RA Koeck J., Oelschlaeger T., Kamp R.M., Braun V.
"Primary structure of colicin M, an inhibitor of murein biosynthesis.", J. Bacteriol. 169:3358-3361(1987).
3D STRUCTURE
PubMed=21149455;DOI=10.1074/jbc.M110.165274
Helbig S., Patzer S.I., Schiene-Fischer C., Zeth K., Braun V.
"Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone.", J.Biol.Chem. 286: 6280-6290 (2011).
PubMed=21149455;DOI=10.1074/jbc.M110.165274
Helbig S., Patzer S.I., Schiene-Fischer C., Zeth K., Braun V.
"Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone.", J.Biol.Chem. 286: 6280-6290 (2011).
Loading...
Gene structure
| Gene id | Name | Description | Location |
| BACGene603 | colicin M activity peptide | 60..875 |
Protein sequence
| ........10 ........20 ........30 ........40 ........50 ........60 ........70 ........80 | | | | | | | | METLTVHAPS PSTNLPSYGN GAFSLSAPHV PGAGPLLVQV VYSFFQSPNM CLQALTQLED YIKKHGASNP LTLQIISTNI GYFCNADRNL VLHPGISVYD AYHFAKPAPS QYDYRSMNMK QMSGNVTTPI VALAHYLWGN GAERSVNIAN IGLKISPMKI NQIKDIIKSG VVGTFPVSTK FTHATGDYNV ITGAYLGNIT LKTEGTLTIS ANGSWTYNGV VRSYDDKYDF NASTHRGIIG ESLTRLGAMF SGKEY |
3D Structure
View PDB entry: 2XMX
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| CHAIN | 1↔271 | 271 | Colicin-M. Feature identifier = PRO_0000218689. |
| MOTIF | 2↔9 | 8 | TonB box. |
| TURN | 11↔13 | 3 | |
| HELIX | 18↔21 | 4 | |
| HELIX | 38↔45 | 8 | |
| HELIX | 49↔65 | 17 | |
| STRAND | 67↔69 | 3 | |
| HELIX | 70↔92 | 23 | |
| HELIX | 98↔104 | 7 | |
| HELIX | 109↔111 | 3 | |
| HELIX | 114↔117 | 4 | |
| STRAND | 120↔122 | 3 | |
| HELIX | 128↔138 | 11 | |
| STRAND | 144↔146 | 3 | |
| HELIX | 148↔150 | 3 | |
| HELIX | 157↔159 | 3 | |
| HELIX | 161↔168 | 8 | |
| STRAND | 173↔184 | 12 | |
| HELIX | 185↔187 | 3 | |
| HELIX | 190↔195 | 6 | |
| STRAND | 198↔209 | 12 | |
| STRAND | 213↔231 | 19 | |
| TURN | 232↔234 | 3 | |
| HELIX | 237↔249 | 13 | |
| STRAND | 255↔258 | 4 | |
| STRAND | 263↔270 | 8 |
Composition
| Amino acid | Count | Percent |
|---|---|---|
| A | 19 | 7.45 % |
| C | 2 | 0.78 % |
| D | 9 | 3.53 % |
| E | 6 | 2.35 % |
| F | 9 | 3.53 % |
| G | 23 | 9.02 % |
| H | 8 | 3.14 % |
| I | 18 | 7.06 % |
| K | 12 | 4.71 % |
| L | 20 | 7.84 % |
| M | 7 | 2.75 % |
| N | 18 | 7.06 % |
| P | 14 | 5.49 % |
| Q | 8 | 3.14 % |
| R | 6 | 2.35 % |
| S | 23 | 9.02 % |
| T | 20 | 7.84 % |
| V | 16 | 6.27 % |
| W | 2 | 0.78 % |
| Y | 15 | 5.88 % |
Hydrophobicity
Composition
| Formula | C1324
H2059
N353
O392
S9 |
| Absent amino acids | |
| Common amino acids | GSLIT |
| Mass (Da) | 29505.15 |
| Net charge | +13 |
| Isoelectric point | 9.5 |
| Basic residues | 30 |
| Acidic residues | 17 |
| Hydrophobic residues | 89 |
| Polar residues | 104 |
| Aliphatic residues | 54 |
| Tiny residues | 65 |
| Boman Index | -276.94 |
| Hydropathy Index | -0.13 |
| Aliphatic Index | 86.01 |
| Instability Index | 38.09 (stable) |
| Half Life |
Mammalian : 30 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 33475 M-1 cm-1 |
| Absorbance 280nm | 123.98 |
