CEAN_ECOLX
ID CEAN_ECOLX Reviewed; 387 AA.
AC P08083;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Colicin-N;
GN Name=cna;
OS Escherichia coli.
OG Plasmid ColN pCHAP4.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2834623; DOI=10.1111/j.1365-2958.1987.tb01938.x;
RA Pugsley A.P.;
RT "Nucleotide sequencing of the structural gene for colicin N reveals
RT homology between the catalytic, C-terminal domains of colicins A and N.";
RL Mol. Microbiol. 1:317-325(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-387.
RX PubMed=3280946; DOI=10.1007/bf00330613;
RA Pugsley A.P.;
RT "The immunity and lysis genes of ColN plasmid pCHAP4.";
RL Mol. Gen. Genet. 211:335-341(1988).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 91-387.
RX PubMed=9687368; DOI=10.1016/s0969-2126(98)00088-4;
RA Vetter I.R., Parker M.W., Tucker A.D., Lakey J.H., Pattus F.,
RA Tsernoglou D.;
RT "Crystal structure of a colicin N fragment suggests a model for toxicity.";
RL Structure 6:863-874(1998).
CC -!- FUNCTION: This colicin is a channel-forming colicin. This class of
CC transmembrane toxins depolarize the cytoplasmic membrane, leading to
CC dissipation of cellular energy.
CC -!- FUNCTION: Colicins are polypeptide toxins produced by and active
CC against E.coli and closely related bacteria.
CC -!- INTERACTION:
CC P08083; P02931: ompF; Xeno; NbExp=3; IntAct=EBI-15691934, EBI-371336;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the channel forming colicin family.
CC {ECO:0000305}.
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DR EMBL; Y00533; CAA68592.1; -; Genomic_DNA.
DR EMBL; X06933; CAA30021.1; -; Genomic_DNA.
DR PIR; S00867; S00867.
DR RefSeq; WP_032488335.1; NZ_VTMM01000024.1.
DR PDB; 1A87; X-ray; 3.10 A; A=67-387.
DR PDBsum; 1A87; -.
DR AlphaFoldDB; P08083; -.
DR BMRB; P08083; -.
DR SASBDB; P08083; -.
DR SMR; P08083; -.
DR DIP; DIP-29645N; -.
DR IntAct; P08083; 1.
DR TCDB; 1.C.1.3.3; the channel-forming colicin (colicin) family.
DR PRIDE; P08083; -.
DR EvolutionaryTrace; P08083; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:CAFA.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:InterPro.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IDA:CAFA.
DR DisProt; DP00461; -.
DR Gene3D; 1.10.490.30; -; 1.
DR InterPro; IPR000293; Channel_colicin_C.
DR InterPro; IPR038283; Channel_colicin_C_sf.
DR Pfam; PF01024; Colicin; 1.
DR PRINTS; PR00280; CHANLCOLICIN.
DR PROSITE; PS00276; CHANNEL_COLICIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Cell membrane;
KW Membrane; Plasmid; Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="Colicin-N"
FT /id="PRO_0000218674"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1A87"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1A87"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1A87"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1A87"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1A87"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1A87"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 170..214
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 352..370
FT /evidence="ECO:0007829|PDB:1A87"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:1A87"
SQ SEQUENCE 387 AA; 41743 MW; 1C4342E222F8CECD CRC64;
MGSNGADNAH NNAFGGGKNP GIGNTSGAGS NGSASSNRGN SNGWSWSNKP HKNDGFHSDG
SYHITFHGDN NSKPKPGGNS GNRGNNGDGA SAKVGEITIT PDNSKPGRYI SSNPEYSLLA
KLIDAESIKG TEVYTFHTRK GQYVKVTVPD SNIDKMRVDY VNWKGPKYNN KLVKRFVSQF
LLFRKEEKEK NEKEALLKAS ELVSGMGDKL GEYLGVKYKN VAKEVANDIK NFHGRNIRSY
NEAMASLNKV LANPKMKVNK SDKDAIVNAW KQVNAKDMAN KIGNLGKAFK VADLAIKVEK
IREKSIEGYN TGNWGPLLLE VESWIIGGVV AGVAISLFGA VLSFLPISGL AVTALGVIGI
MTISYLSSFI DANRVSNINN IISSVIR
