P09167 (AERA_AERHY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aerolysin

Gene names

Name:

aerA

Organism

Aeromonas hydrophila

Taxonomic identifier

644 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis.
Subunit structure	Homodimer in solution; heptamer in the membrane. Ref.4
Subcellular location	Secreted. Host cell membrane.
Sequence similarities	Belongs to the aerolysin family.
Sequence caution	The sequence AAA21938.1 differs from that shown. Reason: Frameshift at position 483.

Ontologies

Keywords
Cellular component	Host cell membrane Host membrane Membrane Secreted
Domain	Signal
Molecular function	Toxin
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane 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

Signal peptide

1 – 23

23

Chain

24 – 445

422

Aerolysin

PRO_0000035620

Propeptide

446 – 493

48

PRO_0000035621

Sites

Site

155

1

Important for oligomerization

Amino acid modifications

Disulfide bond

42 ↔ 98

Disulfide bond

182 ↔ 187

Experimental info

Mutagenesis

244

1

Y → G: Blocks the hemolytic activity. Does not affect the initial structure, the ability to bind to cell-surface receptors or the capacity to form heptamers. But the resulting heptamer is hydrophilic instead of being hydrophobic. Ref.5

Sequence conflict

277

1

E → Q in AAA21938. Ref.1

Sequence conflict

283

1

A → R in AAA21938. Ref.1

Sequence conflict

472

1

A → R in AAA21938. Ref.1

Secondary structure

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493

Helix Strand Turn

Details...

Helix

29 – 31

3

Beta strand

33 – 35

3

Beta strand

46 – 48

3

Helix

51 – 56

6

Helix

58 – 62

5

Beta strand

70 – 72

3

Turn

74 – 76

3

Beta strand

77 – 80

4

Helix

82 – 84

3

Beta strand

88 – 90

3

Beta strand

94 – 102

9

Beta strand

114 – 116

3

Helix

121 – 129

9

Turn

132 – 135

4

Helix

136 – 145

10

Beta strand

162 – 168

7

Beta strand

171 – 176

6

Turn

185 – 188

4

Beta strand

192 – 202

11

Helix

204 – 206

3

Beta strand

213 – 229

17

Beta strand

231 – 233

3

Beta strand

237 – 252

16

Helix

257 – 260

4

Beta strand

274 – 276

3

Beta strand

284 – 286

3

Helix

288 – 290

3

Beta strand

293 – 304

12

Beta strand

312 – 345

34

Beta strand

352 – 354

3

Beta strand

361 – 370

10

Helix

374 – 376

3

Helix

378 – 384

7

Helix

388 – 390

3

Beta strand

392 – 394

3

Helix

396 – 403

8

Helix

405 – 415

11

Beta strand

419 – 434

16

Beta strand

465 – 467

3

Helix

472 – 477

6

Beta strand

481 – 489

9

Sequences

	Sequence		Length	Mass (Da)
	P09167 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: D396CE4EAD85AEF0	FASTA	493	54,342
	10 20 30 40 50 60 MQKIKLTGLS LIISGLLMAQ AQAAEPVYPD QLRLFSLGQG VCGDKYRPVN REEAQSVKSN 70 80 90 100 110 120 IVGMMGQWQI SGLANGWVIM GPGYNGEIKP GTASNTWCYP TNPVTGEIPT LSALDIPDGD 130 140 150 160 170 180 EVDVQWRLVH DSANFIKPTS YLAHYLGYAW VGGNHSQYVG EDMDVTRDGD GWVIRGNNDG 190 200 210 220 230 240 GCDGYRCGDK TAIKVSNFAY NLDPDSFKHG DVTQSDRQLV KTVVGWAVND SDTPQSGYDV 250 260 270 280 290 300 TLRYDTATNW SKTNTYGLSE KVTTKNKFKW PLVGETELSI EIAANQSWAS QNGGSTTTSL 310 320 330 340 350 360 SQSVRPTVPA RSKIPVKIEL YKADISYPYE FKADVSYDLT LSGFLRWGGN AWYTHPDNRP 370 380 390 400 410 420 NWNHTFVIGP YKDKASSIRY QWDKRYIPGE VKWWDWNWTI QQNGLSTMQN NLARVLRPVR 430 440 450 460 470 480 AGITGDFSAE SQFAGNIEIG APVPLAADSK VRRARSVDGA GQGLRLEIPL DAQELSGLGF 490 NNVSLSVTPA ANQ

References

[1]	"Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila." Howard S.P., Garland W.J., Green M.J., Buckley J.T. J. Bacteriol. 169:2869-2871(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Molecular cloning and expression in Escherichia coli of the structural gene for the hemolytic toxin aerolysin from Aeromonas hydrophila." Howard S.P., Buckley J.T. Mol. Gen. Genet. 204:289-295(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
[3]	"Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation." van der Goot F.G., Lakey J., Pattus F., Kay C.M., Sorokine O., van Dorsselaer A., Buckley J.T. Biochemistry 31:8566-8570(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Protonation of histidine-132 promotes oligomerization of the channel-forming toxin aerolysin." Buckley J.T., Wilmsen H.U., Lesieur C., Schulze A., Pattus F., Parker M.W., van der Goot F.G. Biochemistry 34:16450-16455(1995) [PubMed] [Europe PMC] [Abstract] Cited for: IMPORTANCE OF HIS-155 FOR OLIGOMERIZATION.
[5]	"Conversion of a transmembrane to a water-soluble protein complex by a single point mutation." Tsitrin Y., Morton C.J., el-Bez C., Paumard P., Velluz M.C., Adrian M., Dubochet J., Parker M.W., Lanzavecchia S., van der Goot F.G. Nat. Struct. Biol. 9:729-733(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-244.
[6]	"Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states." Parker M.W., Buckley J.T., Postma J.P., Tucker A.D., Leonard K., Pattus F., Tsernoglou D. Nature 367:292-295(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16495 Genomic DNA. Translation: AAA21938.1. Frameshift.
M29818 Genomic DNA. Translation: AAA21934.1.

PIR

A25976.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PRE	X-ray	2.80	A/B	24-493	[»]
1Z52	X-ray	2.38	A/B	24-493	[»]
3C0M	X-ray	2.88	A/B	24-493	[»]
3C0N	X-ray	2.20	A/B	24-493	[»]
3C0O	X-ray	2.50	A/B	24-493	[»]
3G4N	X-ray	2.10	A/B	24-493	[»]
3G4O	X-ray	2.30	A/B	24-493	[»]

ProteinModelPortal

P09167.

SMR

P09167. Positions 25-491.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1958193.

Protein family/group databases

TCDB

1.C.4.1.1. aerolysin channel-forming toxin (Aerolysin) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.170.15.10. 1 hit.
3.10.40.10. 1 hit.

InterPro

IPR005832. Aerolysin.
IPR023307. Aerolysin-like_beta_cmplx_dom.
IPR005831. Aerolysin/haemolysin_CS.
IPR005830. Aerolysn_hemolysn_leukocdn_tox.
IPR005138. APT.
IPR016187. C-type_lectin_fold.
[Graphical view]

Pfam

PF01117. Aerolysin. 1 hit.
PF03440. APT. 1 hit.
[Graphical view]

PRINTS

PR00754. AEROLYSIN.

SMART

SM00999. Aerolysin. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00274. AEROLYSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09167.

PMAP-CutDB

P09167.

Entry information

Entry name

AERA_AERHY

Accession

Primary (citable) accession number: P09167

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program