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Protein

Enterotoxin type C-2

Gene

entC2

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc
Metal bindingi110 – 1101Zinc
Metal bindingi145 – 1451Zinc
Metal bindingi149 – 1491Zinc

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Enterotoxin, Superantigen, Toxin

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Enterotoxin type C-2
Alternative name(s):
SEC2
Gene namesi
Name:entC2
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei2141. Sta a SEC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 266239Enterotoxin type C-2PRO_0000035608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi120 ↔ 137

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP34071.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV2009.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 373Combined sources
Helixi41 – 433Combined sources
Helixi49 – 524Combined sources
Turni53 – 553Combined sources
Beta strandi60 – 656Combined sources
Beta strandi75 – 795Combined sources
Turni83 – 853Combined sources
Beta strandi89 – 946Combined sources
Helixi98 – 1047Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 1454Combined sources
Helixi151 – 1533Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi168 – 18215Combined sources
Helixi183 – 19816Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi231 – 2333Combined sources
Helixi237 – 2415Combined sources
Helixi242 – 2443Combined sources
Beta strandi249 – 2513Combined sources
Turni252 – 2543Combined sources
Beta strandi256 – 2627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQVX-ray2.06A28-266[»]
1I4PX-ray2.00A28-266[»]
1I4QX-ray2.20A28-266[»]
1I4RX-ray2.10A28-266[»]
1I4XX-ray2.40A28-266[»]
1SE2X-ray2.70A28-266[»]
1STEX-ray2.00A28-266[»]
1UNSX-ray2.00A28-266[»]
ProteinModelPortaliP34071.
SMRiP34071. Positions 28-264.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34071.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.20.120. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR006126. Staph/Strept_toxin_CS.
IPR006173. Staph_tox_OB.
IPR016091. SuperAg_toxin_C.
IPR013307. Superantigen_bac.
IPR006123. Toxin_b-grasp_Staph/Strep.
IPR006177. Toxin_bac.
[Graphical view]
PfamiPF02876. Stap_Strp_tox_C. 1 hit.
PF01123. Stap_Strp_toxin. 1 hit.
[Graphical view]
PRINTSiPR00279. BACTRLTOXIN.
PR01898. SAGSUPRFAMLY.
SUPFAMiSSF50203. SSF50203. 1 hit.
SSF54334. SSF54334. 1 hit.
PROSITEiPS00277. STAPH_STREP_TOXIN_1. 1 hit.
PS00278. STAPH_STREP_TOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34071-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKSRFISCV ILIFALILVL FTPNVLAESQ PDPTPDELHK SSEFTGTMGN
60 70 80 90 100
MKYLYDDHYV SATKVMSVDK FLAHDLIYNI SDKKLKNYDK VKTELLNEDL
110 120 130 140 150
AKKYKDEVVD VYGSNYYVNC YFSSKDNVGK VTGGKTCMYG GITKHEGNHF
160 170 180 190 200
DNGNLQNVLI RVYENKRNTI SFEVQTDKKS VTAQELDIKA RNFLINKKNL
210 220 230 240 250
YEFNSSPYET GYIKFIENNG NTFWYDMMPA PGDKFDQSKY LMMYNDNKTV
260
DSKSVKIEVH LTTKNG
Length:266
Mass (Da):30,604
Last modified:February 1, 1994 - v1
Checksum:i8407FB18536FAC08
GO

Sequence databases

PIRiA60114.
RefSeqiWP_001043552.1. NZ_LSMV01000010.1.

Cross-referencesi

Sequence databases

PIRiA60114.
RefSeqiWP_001043552.1. NZ_LSMV01000010.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQVX-ray2.06A28-266[»]
1I4PX-ray2.00A28-266[»]
1I4QX-ray2.20A28-266[»]
1I4RX-ray2.10A28-266[»]
1I4XX-ray2.40A28-266[»]
1SE2X-ray2.70A28-266[»]
1STEX-ray2.00A28-266[»]
1UNSX-ray2.00A28-266[»]
ProteinModelPortaliP34071.
SMRiP34071. Positions 28-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV2009.

Protein family/group databases

Allergomei2141. Sta a SEC.

Proteomic databases

PaxDbiP34071.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP34071.
PROiP34071.

Family and domain databases

Gene3Di3.10.20.120. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR006126. Staph/Strept_toxin_CS.
IPR006173. Staph_tox_OB.
IPR016091. SuperAg_toxin_C.
IPR013307. Superantigen_bac.
IPR006123. Toxin_b-grasp_Staph/Strep.
IPR006177. Toxin_bac.
[Graphical view]
PfamiPF02876. Stap_Strp_tox_C. 1 hit.
PF01123. Stap_Strp_toxin. 1 hit.
[Graphical view]
PRINTSiPR00279. BACTRLTOXIN.
PR01898. SAGSUPRFAMLY.
SUPFAMiSSF50203. SSF50203. 1 hit.
SSF54334. SSF54334. 1 hit.
PROSITEiPS00277. STAPH_STREP_TOXIN_1. 1 hit.
PS00278. STAPH_STREP_TOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Conservation of the biologically active portions of staphylococcal enterotoxins C1 and C2."
    Bohach G.A., Schlievert P.M.
    Infect. Immun. 57:2249-2252(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-66.
  2. "Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site."
    Papageorgiou A.C., Acharya K.R., Shapiro R., Passalacqua E.F., Brehm R.D., Tranter H.S.
    Structure 3:769-779(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  3. "Residues defining V beta specificity in staphylococcal enterotoxins."
    Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.
    Nat. Struct. Biol. 2:680-686(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  4. "A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity."
    Schad E.M., Papageorgiou A.C., Svensson L.A., Acharya K.R.
    J. Mol. Biol. 269:270-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPARISON OF STRUCTURE OF SEA AND SEC2.

Entry informationi

Entry nameiENTC2_STAAU
AccessioniPrimary (citable) accession number: P34071
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.