TOXA_PASMD
ID TOXA_PASMD Reviewed; 1285 AA.
AC P17452; Q57008;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Dermonecrotic toxin;
DE Short=DNT;
DE AltName: Full=Mitogenic toxin;
DE AltName: Full=PMT;
GN Name=toxA;
OS Pasteurella multocida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCTC 12178;
RX PubMed=2201870; DOI=10.1111/j.1365-2958.1990.tb00652.x;
RA Petersen S.K.;
RT "The complete nucleotide sequence of the Pasteurella multocida toxin gene
RT and evidence for a transcriptional repressor, TxaR.";
RL Mol. Microbiol. 4:821-830(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CVI 47459;
RX PubMed=2339066; DOI=10.1093/nar/18.9.2815;
RA Buys W.E.C.M., Smith H.E., Kamps A.M.I.E., Kamp E.M., Smits M.A.;
RT "Sequence of the dermonecrotic toxin of Pasteurella multocida ssp.
RT multocida.";
RL Nucleic Acids Res. 18:2815-2816(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LFB3;
RX PubMed=2269370; DOI=10.1016/0014-5793(90)80809-w;
RA Lax A.J., Chanter N., Pullinger G.D., Higgins T., Staddon J.M.,
RA Rozengurt E.;
RT "Sequence analysis of the potent mitogenic toxin of Pasteurella
RT multocida.";
RL FEBS Lett. 277:59-64(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH05;
RA Chang G.-N., Ho K.-C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a dermonecrotic toxin. This osteolytic toxin, induces
CC bone resorption. Potent mitogen. This toxin is associated with the
CC severe progressive form of the atrophic rhinitis, a major respiratory
CC disease in pigs.
CC -!- INTERACTION:
CC P17452; P20152: Vim; Xeno; NbExp=4; IntAct=EBI-9541048, EBI-299269;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Secreted {ECO:0000305}.
CC Host membrane {ECO:0000305}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Closely spaced cysteine and histidine residues may
CC provide the toxin with an affinity for metal.
CC -!- MISCELLANEOUS: The sequence shown is that of strain NCTC 12178.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51512; CAA35885.1; -; Genomic_DNA.
DR EMBL; X52478; CAA36717.1; -; Genomic_DNA.
DR EMBL; Z28388; CAA82233.1; -; Genomic_DNA.
DR EMBL; X57775; CAA40921.1; -; Genomic_DNA.
DR EMBL; AF240778; AAL55665.1; -; Genomic_DNA.
DR PIR; S12998; BTQPD.
DR PDB; 2EBF; X-ray; 1.90 A; X=569-1285.
DR PDB; 2EBH; X-ray; 2.40 A; X=569-1285.
DR PDB; 2EC5; X-ray; 2.60 A; A/B=569-1285.
DR PDB; 2N9V; NMR; -; A=589-668.
DR PDBsum; 2EBF; -.
DR PDBsum; 2EBH; -.
DR PDBsum; 2EC5; -.
DR PDBsum; 2N9V; -.
DR AlphaFoldDB; P17452; -.
DR BMRB; P17452; -.
DR SMR; P17452; -.
DR IntAct; P17452; 2.
DR TCDB; 1.C.57.3.1; the clostridial cytotoxin (cct) family.
DR EvolutionaryTrace; P17452; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IMP:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IMP:AgBase.
DR GO; GO:0005543; F:phospholipid binding; IMP:AgBase.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0001907; P:killing by symbiont of host cells; IDA:CACAO.
DR GO; GO:1990216; P:positive regulation by symbiont of host transcription; IMP:AgBase.
DR InterPro; IPR020972; Dermonecrotic/RTX_toxin_MLD.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF11647; MLD; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Host membrane; Membrane; Secreted; Toxin;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..1285
FT /note="Dermonecrotic toxin"
FT /id="PRO_0000072635"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 853
FT /note="F -> Y (in strain: CVI 47459)"
FT CONFLICT 304
FT /note="A -> R (in Ref. 1; CAA35885)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="A -> R (in Ref. 1; CAA35885)"
FT /evidence="ECO:0000305"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:2EC5"
FT HELIX 593..599
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:2N9V"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:2N9V"
FT HELIX 627..647
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 650..653
FT /evidence="ECO:0007829|PDB:2N9V"
FT HELIX 654..668
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 674..682
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 690..702
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 710..719
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 721..724
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 749..753
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 763..765
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 766..769
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 773..787
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 799..802
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 806..812
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 815..817
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 827..839
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 844..848
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 851..872
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 878..884
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 889..895
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 898..907
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 910..916
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 918..926
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 928..933
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 938..945
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 946..957
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 964..973
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 974..976
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 981..991
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 995..1000
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1012..1029
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1037..1041
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1043..1046
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1049..1056
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1059..1063
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1067..1070
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1076..1078
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1083..1085
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1103..1107
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1110..1112
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1116..1119
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1122..1130
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1135..1149
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1152..1156
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 1162..1164
FT /evidence="ECO:0007829|PDB:2EBH"
FT HELIX 1168..1178
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1187..1195
FT /evidence="ECO:0007829|PDB:2EBF"
FT TURN 1196..1198
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1199..1212
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1215..1220
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1223..1225
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1230..1232
FT /evidence="ECO:0007829|PDB:2EC5"
FT STRAND 1234..1239
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1240..1250
FT /evidence="ECO:0007829|PDB:2EBF"
FT STRAND 1254..1261
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1265..1269
FT /evidence="ECO:0007829|PDB:2EBF"
FT HELIX 1275..1277
FT /evidence="ECO:0007829|PDB:2EBF"
SQ SEQUENCE 1285 AA; 146383 MW; E67A9FCA58C107DA CRC64;
MKTKHFFNSD FTVKGKSADE IFRRLCTDHP DKQLNNVKWK EVFINRFGQM MLDTPNPRKI
VEKIINEGLE KQGLKNIDPE TTYFNIFSSS DSSDGNVFHY NSLSESYRVT DACLMNIFVE
RYFDDWDLLN SLASNGIYSV GKEGAYYPDH DYGPEYNPVW GPNEQIYHSR VIADILYARS
VWDEFKKYFM EYWQKYAQLY TEMLSDTFLA MAIQQYTRQT LTDEGFLMVC NTYYGNKEEV
QITLLDIYGY PSTDIICIEQ KGLPTPKVIL YIPGGTQPFV EFLNTDDLKQ WIAWHLKDNK
HMVAFRKHFS LKQRQEGETF TGIDKALQYI AEESPEWPAN KYILYNPTHL ETENLFNIMM
KRTEQRMLED SDVQIRSNSE ATRDYALSLL ETFISQLSAI DMLVPAVGIP INFALSATAL
GLSSDIVVNG DSYEKRKYGI GSLVQSALFT GINLIPVISE TAEILSSFSR TEEDIPAFFT
EEQALAQRFE IVEEELHSIS PDDPPREITD ENLHKIRLVR LNNENQPLVV LRRLGGNKFI
RIEPITFQEI KGSLVSEVIN PVTNKTYYVS NAKLLGGSPY SPFRIGLEGV WTPEVLKARA
SVIGKPIGES YKRILAKLQR IHNSNILDER QGLMHELMEL IDLYEESQPS SERLNAFREL
RTQLEKALYL PEMEALKKQI LQIPNKGSGA ARFLLRTAMN EMAGKTSEST ADLIRFALQD
TVISAPFRGY AGAIPEAIDF PVKYVIEDIS VFDKIQTNYW ELPAYESWNE GSNSALLPGL
LRESQSKGML SKCRIIENSL YIGHSYEEMF YSISPYSNQV GGPYELYPFT FFSMLQEVQG
DLGFEQAFAT RNFFNTLVSD RLSLMENTML LTESFDYTPW DAIYGDINYD EQFAAMSINE
RIEKCMNTYR GVAFQNSSKS IDFFLNNLTT FIDNGLTEIA ISDLPYDIVQ QEISQFLQGS
NEWKTLDAML FNLDKGDING AFRKLLQSAK DNNIKFRAIG HSDNSVPPFN NPYKSLYYKG
NIIAEAIEKL DREGQKFVVF ADSSLLNSTP GTGRPMPGLV QYLKIPATVV DSDGAWQFLP
DVASSRVPIE VTELENWQVL TPPQGKILGL KQFKLTAGFP TEQSRLPLLE NSVSEDLREE
LMQKIDAIKN DVKMNSLVCM EAGSCDSVSP KVAARLKDMG LEAGMGASIT WWRREGGMEF
SHQMHTTASF KFAGKEFAVD ASHLQFVHDQ LDTTILILPV DDWALEIAQR NRAINPFVEY
VSKTGNMLAL FMPPLFTKPR LTRAL
