Reviewed, UniProtKB/Swiss-Prot P08083 (CEAN_ECOLX)

Names and origin

Protein names

Recommended name:
    Colicin-N

Gene names

Name:

cna

Encoded on

Plasmid ColN pCHAP4

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the channel forming colicin family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Antibiotic Antimicrobial Bacteriocin
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to Gram-negative bacterium Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	receptor binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 387

387

Colicin-N

PRO_0000218674

Regions

Transmembrane

325 – 345

21

Potential

Transmembrane

350 – 370

21

Potential

Compositional bias

1 – 49

49

Gly-rich

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

387

Helix Strand Turn

Details...

Beta strand

97 – 101

5

Beta strand

108 – 112

5

Helix

114 – 116

3

Turn

117 – 119

3

Beta strand

121 – 128

8

Beta strand

131 – 137

7

Beta strand

143 – 148

6

Helix

149 – 151

3

Helix

153 – 155

3

Beta strand

157 – 162

6

Helix

170 – 214

45

Helix

216 – 230

15

Helix

234 – 236

3

Helix

240 – 251

12

Helix

260 – 271

12

Helix

275 – 283

9

Helix

287 – 289

3

Helix

294 – 309

16

Helix

315 – 326

12

Helix

331 – 343

13

Helix

352 – 370

19

Helix

372 – 385

14

Sequences

	Sequence		Length	Mass (Da)
	P08083-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 1C4342E222F8CECD	FASTA	387	41,743
	10 20 30 40 50 60 MGSNGADNAH NNAFGGGKNP GIGNTSGAGS NGSASSNRGN SNGWSWSNKP HKNDGFHSDG 70 80 90 100 110 120 SYHITFHGDN NSKPKPGGNS GNRGNNGDGA SAKVGEITIT PDNSKPGRYI SSNPEYSLLA 130 140 150 160 170 180 KLIDAESIKG TEVYTFHTRK GQYVKVTVPD SNIDKMRVDY VNWKGPKYNN KLVKRFVSQF 190 200 210 220 230 240 LLFRKEEKEK NEKEALLKAS ELVSGMGDKL GEYLGVKYKN VAKEVANDIK NFHGRNIRSY 250 260 270 280 290 300 NEAMASLNKV LANPKMKVNK SDKDAIVNAW KQVNAKDMAN KIGNLGKAFK VADLAIKVEK 310 320 330 340 350 360 IREKSIEGYN TGNWGPLLLE VESWIIGGVV AGVAISLFGA VLSFLPISGL AVTALGVIGI 370 380 MTISYLSSFI DANRVSNINN IISSVIR

References

[1]	"Nucleotide sequencing of the structural gene for colicin N reveals homology between the catalytic, C-terminal domains of colicins A and N." Pugsley A.P. Mol. Microbiol. 1:317-325(1987) [PubMed: 2834623] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The immunity and lysis genes of ColN plasmid pCHAP4." Pugsley A.P. Mol. Gen. Genet. 211:335-341(1988) [PubMed: 3280946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-387.
[3]	"Crystal structure of a colicin N fragment suggests a model for toxicity." Vetter I.R., Parker M.W., Tucker A.D., Lakey J.H., Pattus F., Tsernoglou D. Structure 6:863-874(1998) [PubMed: 9687368] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 91-387.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00533 Genomic DNA. Translation: CAA68592.1.
X06933 Genomic DNA. Translation: CAA30021.1.

PIR

S00867.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A87	X-ray	3.10	A	67-387	[»]

DisProt

DP00461.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29645N.

Protein family/group databases

TCDB

1.C.1.3.3. channel-forming colicin family.

Family and domain databases

InterPro

IPR000293. Channel_colicin_C.
[Graphical view]

Gene3D

G3DSA:1.10.490.30. Channel_colicin_C. 1 hit.

Pfam

PF01024. Colicin. 1 hit.
[Graphical view]

PRINTS

PR00280. CHANLCOLICIN.

ProDom

PD002657. Channel_colicin_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00276. CHANNEL_COLICIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CEAN_ECOLX

Accession

Primary (citable) accession number: P08083

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	December 15, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)