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Protein

Dermonecrotic toxin

Gene

toxA

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

Functioni

This is a dermonecrotic toxin. This osteolytic toxin, induces bone resorption. Potent mitogen. This toxin is associated with the severe progressive form of the atrophic rhinitis, a major respiratory disease in pigs.

GO - Molecular functioni

  • phospholipase activity Source: AgBase
  • phospholipid binding Source: AgBase

GO - Biological processi

  • killing by symbiont of host cells Source: CACAO
  • positive regulation by symbiont of host transcription Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Protein family/group databases

TCDBi1.C.57.3.1. the clostridial cytotoxin (cct) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Dermonecrotic toxin
Short name:
DNT
Alternative name(s):
Mitogenic toxin
PMT
Gene namesi
Name:toxA
OrganismiPasteurella multocida
Taxonomic identifieri747 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei402 – 42221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB-SubCell
  • host cell plasma membrane Source: AgBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Host membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12851285Dermonecrotic toxinPRO_0000072635Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
VimP201524EBI-9541048,EBI-299269From a different organism.

Protein-protein interaction databases

IntActiP17452. 2 interactions.

Structurei

Secondary structure

1
1285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi578 – 5803Combined sources
Helixi593 – 5997Combined sources
Helixi609 – 62315Combined sources
Helixi627 – 64721Combined sources
Helixi654 – 66815Combined sources
Helixi671 – 6733Combined sources
Helixi674 – 6829Combined sources
Helixi690 – 70213Combined sources
Helixi710 – 71910Combined sources
Turni721 – 7244Combined sources
Beta strandi744 – 7474Combined sources
Helixi749 – 7535Combined sources
Beta strandi754 – 7563Combined sources
Turni759 – 7613Combined sources
Helixi763 – 7653Combined sources
Turni766 – 7694Combined sources
Helixi773 – 78715Combined sources
Beta strandi788 – 7903Combined sources
Beta strandi793 – 7964Combined sources
Beta strandi799 – 8024Combined sources
Helixi806 – 8127Combined sources
Turni815 – 8173Combined sources
Beta strandi822 – 8243Combined sources
Helixi827 – 83913Combined sources
Helixi844 – 8485Combined sources
Helixi851 – 87222Combined sources
Helixi878 – 8847Combined sources
Helixi889 – 8957Combined sources
Helixi898 – 90710Combined sources
Beta strandi910 – 9167Combined sources
Helixi918 – 9269Combined sources
Helixi928 – 9336Combined sources
Beta strandi938 – 9458Combined sources
Helixi946 – 95712Combined sources
Helixi964 – 97310Combined sources
Turni974 – 9763Combined sources
Helixi981 – 99111Combined sources
Beta strandi995 – 10006Combined sources
Helixi1012 – 102918Combined sources
Beta strandi1037 – 10415Combined sources
Helixi1043 – 10464Combined sources
Beta strandi1049 – 10568Combined sources
Helixi1059 – 10635Combined sources
Beta strandi1067 – 10704Combined sources
Beta strandi1076 – 10783Combined sources
Helixi1083 – 10853Combined sources
Beta strandi1086 – 10883Combined sources
Beta strandi1103 – 11075Combined sources
Beta strandi1110 – 11123Combined sources
Beta strandi1116 – 11194Combined sources
Helixi1122 – 11309Combined sources
Helixi1135 – 114915Combined sources
Helixi1152 – 11565Combined sources
Turni1162 – 11643Combined sources
Helixi1168 – 117811Combined sources
Beta strandi1187 – 11959Combined sources
Turni1196 – 11983Combined sources
Beta strandi1199 – 121214Combined sources
Beta strandi1215 – 12206Combined sources
Helixi1223 – 12253Combined sources
Beta strandi1230 – 12323Combined sources
Beta strandi1234 – 12396Combined sources
Helixi1240 – 125011Combined sources
Beta strandi1254 – 12618Combined sources
Helixi1265 – 12695Combined sources
Helixi1275 – 12773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBFX-ray1.90X569-1285[»]
2EBHX-ray2.40X569-1285[»]
2EC5X-ray2.60A/B569-1285[»]
ProteinModelPortaliP17452.
SMRiP17452. Positions 575-1285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17452.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR020972. Dermonecrotic/RTX_toxin_C.
[Graphical view]
PfamiPF11647. PMT_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTKHFFNSD FTVKGKSADE IFRRLCTDHP DKQLNNVKWK EVFINRFGQM
60 70 80 90 100
MLDTPNPRKI VEKIINEGLE KQGLKNIDPE TTYFNIFSSS DSSDGNVFHY
110 120 130 140 150
NSLSESYRVT DACLMNIFVE RYFDDWDLLN SLASNGIYSV GKEGAYYPDH
160 170 180 190 200
DYGPEYNPVW GPNEQIYHSR VIADILYARS VWDEFKKYFM EYWQKYAQLY
210 220 230 240 250
TEMLSDTFLA MAIQQYTRQT LTDEGFLMVC NTYYGNKEEV QITLLDIYGY
260 270 280 290 300
PSTDIICIEQ KGLPTPKVIL YIPGGTQPFV EFLNTDDLKQ WIAWHLKDNK
310 320 330 340 350
HMVAFRKHFS LKQRQEGETF TGIDKALQYI AEESPEWPAN KYILYNPTHL
360 370 380 390 400
ETENLFNIMM KRTEQRMLED SDVQIRSNSE ATRDYALSLL ETFISQLSAI
410 420 430 440 450
DMLVPAVGIP INFALSATAL GLSSDIVVNG DSYEKRKYGI GSLVQSALFT
460 470 480 490 500
GINLIPVISE TAEILSSFSR TEEDIPAFFT EEQALAQRFE IVEEELHSIS
510 520 530 540 550
PDDPPREITD ENLHKIRLVR LNNENQPLVV LRRLGGNKFI RIEPITFQEI
560 570 580 590 600
KGSLVSEVIN PVTNKTYYVS NAKLLGGSPY SPFRIGLEGV WTPEVLKARA
610 620 630 640 650
SVIGKPIGES YKRILAKLQR IHNSNILDER QGLMHELMEL IDLYEESQPS
660 670 680 690 700
SERLNAFREL RTQLEKALYL PEMEALKKQI LQIPNKGSGA ARFLLRTAMN
710 720 730 740 750
EMAGKTSEST ADLIRFALQD TVISAPFRGY AGAIPEAIDF PVKYVIEDIS
760 770 780 790 800
VFDKIQTNYW ELPAYESWNE GSNSALLPGL LRESQSKGML SKCRIIENSL
810 820 830 840 850
YIGHSYEEMF YSISPYSNQV GGPYELYPFT FFSMLQEVQG DLGFEQAFAT
860 870 880 890 900
RNFFNTLVSD RLSLMENTML LTESFDYTPW DAIYGDINYD EQFAAMSINE
910 920 930 940 950
RIEKCMNTYR GVAFQNSSKS IDFFLNNLTT FIDNGLTEIA ISDLPYDIVQ
960 970 980 990 1000
QEISQFLQGS NEWKTLDAML FNLDKGDING AFRKLLQSAK DNNIKFRAIG
1010 1020 1030 1040 1050
HSDNSVPPFN NPYKSLYYKG NIIAEAIEKL DREGQKFVVF ADSSLLNSTP
1060 1070 1080 1090 1100
GTGRPMPGLV QYLKIPATVV DSDGAWQFLP DVASSRVPIE VTELENWQVL
1110 1120 1130 1140 1150
TPPQGKILGL KQFKLTAGFP TEQSRLPLLE NSVSEDLREE LMQKIDAIKN
1160 1170 1180 1190 1200
DVKMNSLVCM EAGSCDSVSP KVAARLKDMG LEAGMGASIT WWRREGGMEF
1210 1220 1230 1240 1250
SHQMHTTASF KFAGKEFAVD ASHLQFVHDQ LDTTILILPV DDWALEIAQR
1260 1270 1280
NRAINPFVEY VSKTGNMLAL FMPPLFTKPR LTRAL
Length:1,285
Mass (Da):146,383
Last modified:April 27, 2001 - v2
Checksum:iE67A9FCA58C107DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041A → R in CAA35885 (PubMed:2201870).Curated
Sequence conflicti775 – 7751A → R in CAA35885 (PubMed:2201870).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti853 – 8531F → Y in strain: CVI 47459.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51512 Genomic DNA. Translation: CAA35885.1.
X52478 Genomic DNA. Translation: CAA36717.1.
Z28388 Genomic DNA. Translation: CAA82233.1.
X57775 Genomic DNA. Translation: CAA40921.1.
AF240778 Genomic DNA. Translation: AAL55665.1.
PIRiS12998. BTQPD.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51512 Genomic DNA. Translation: CAA35885.1.
X52478 Genomic DNA. Translation: CAA36717.1.
Z28388 Genomic DNA. Translation: CAA82233.1.
X57775 Genomic DNA. Translation: CAA40921.1.
AF240778 Genomic DNA. Translation: AAL55665.1.
PIRiS12998. BTQPD.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBFX-ray1.90X569-1285[»]
2EBHX-ray2.40X569-1285[»]
2EC5X-ray2.60A/B569-1285[»]
ProteinModelPortaliP17452.
SMRiP17452. Positions 575-1285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17452. 2 interactions.

Protein family/group databases

TCDBi1.C.57.3.1. the clostridial cytotoxin (cct) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP17452.

Family and domain databases

InterProiIPR020972. Dermonecrotic/RTX_toxin_C.
[Graphical view]
PfamiPF11647. PMT_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete nucleotide sequence of the Pasteurella multocida toxin gene and evidence for a transcriptional repressor, TxaR."
    Petersen S.K.
    Mol. Microbiol. 4:821-830(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCTC 12178.
  2. "Sequence of the dermonecrotic toxin of Pasteurella multocida ssp. multocida."
    Buys W.E.C.M., Smith H.E., Kamps A.M.I.E., Kamp E.M., Smits M.A.
    Nucleic Acids Res. 18:2815-2816(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CVI 47459.
  3. "Sequence analysis of the potent mitogenic toxin of Pasteurella multocida."
    Lax A.J., Chanter N., Pullinger G.D., Higgins T., Staddon J.M., Rozengurt E.
    FEBS Lett. 277:59-64(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LFB3.
  4. Chang G.-N., Ho K.-C.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CH05.

Entry informationi

Entry nameiTOXA_PASMD
AccessioniPrimary (citable) accession number: P17452
Secondary accession number(s): Q57008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: April 27, 2001
Last modified: December 9, 2015
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Closely spaced cysteine and histidine residues may provide the toxin with an affinity for metal.
The sequence shown is that of strain NCTC 12178.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.