LUKDV_STAA8
ID LUKDV_STAA8 Reviewed; 327 AA.
AC Q2FXB1;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Leucotoxin LukDv;
DE AltName: Full=Variant of LukD;
DE Flags: Precursor;
GN Name=lukDv; OrderedLocusNames=SAOUHSC_01954;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 27733 / V8;
RX PubMed=12636257; DOI=10.1111/j.1348-0421.2003.tb02789.x;
RA Morinaga N., Kaihou Y., Noda M.;
RT "Purification, cloning and characterization of variant LukE-LukD with
RT strong leukocidal activity of staphylococcal bi-component leukotoxin
RT family.";
RL Microbiol. Immunol. 47:81-90(2003).
RN [3]
RP SIMILARITY TO LUKDV.
RX PubMed=15170101; DOI=10.1271/bbb.68.981;
RA Kaneko J., Kamio Y.;
RT "Bacterial two-component and hetero-heptameric pore-forming cytolytic
RT toxins: structures, pore-forming mechanism, and organization of the
RT genes.";
RL Biosci. Biotechnol. Biochem. 68:981-1003(2004).
CC -!- FUNCTION: Part of a bi-component leucotoxin that acts by forming pores
CC in the membrane of the target cells. The activity of LukEv-LukDv to
CC rabbit leukocytes is similar to that of the Panton-Valentine leucocidin
CC (PVL). LukEv-LukDv is hemolytic to rabbit red blood cells although the
CC activity is only 8% of gamma-hemolysin. {ECO:0000269|PubMed:12636257}.
CC -!- SUBUNIT: Toxicity requires sequential binding and synergistic
CC association of a class S and a class F component which form
CC heterooligomeric complexes (By similarity). LukEv (class S) associates
CC with LukDv (class F). {ECO:0000250, ECO:0000269|PubMed:12636257}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR EMBL; CP000253; ABD31015.1; -; Genomic_DNA.
DR RefSeq; WP_000782464.1; NZ_LS483365.1.
DR RefSeq; YP_500453.1; NC_007795.1.
DR PDB; 6U2S; X-ray; 1.50 A; A=27-327.
DR PDB; 6U33; X-ray; 1.75 A; A=27-327.
DR PDBsum; 6U2S; -.
DR PDBsum; 6U33; -.
DR AlphaFoldDB; Q2FXB1; -.
DR SMR; Q2FXB1; -.
DR STRING; 1280.SAXN108_1856; -.
DR EnsemblBacteria; ABD31015; ABD31015; SAOUHSC_01954.
DR GeneID; 3920899; -.
DR KEGG; sao:SAOUHSC_01954; -.
DR PATRIC; fig|93061.5.peg.1779; -.
DR eggNOG; ENOG50348U0; Bacteria.
DR HOGENOM; CLU_055394_0_1_9; -.
DR OMA; DYSQFYW; -.
DR PRO; PR:Q2FXB1; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR003963; Bi-component_toxin_staph.
DR InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR Pfam; PF07968; Leukocidin; 1.
DR PRINTS; PR01468; BICOMPNTOXIN.
DR SUPFAM; SSF56959; SSF56959; 1.
DR TIGRFAMs; TIGR01002; hlyII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Hemolysis; Reference proteome; Secreted; Signal;
KW Toxin; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..327
FT /note="Leucotoxin LukDv"
FT /id="PRO_0000419804"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 34..53
FT /evidence="ECO:0007829|PDB:6U2S"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 73..86
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 98..116
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:6U2S"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6U2S"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6U33"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6U2S"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6U2S"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6U2S"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6U2S"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 265..282
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 287..307
FT /evidence="ECO:0007829|PDB:6U2S"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:6U2S"
FT STRAND 312..324
FT /evidence="ECO:0007829|PDB:6U2S"
SQ SEQUENCE 327 AA; 36889 MW; 3807DB6421ACDAAA CRC64;
MKMKKLVKSS VASSIALLLL SNTVDAAQHI TPVSEKKVDD KITLYKTTAT SDNDKLNISQ
ILTFNFIKDK SYDKDTLVLK AAGNINSGYK KPNPKDYNYS QFYWGGKYNV SVSSESNDAV
NVVDYAPKNQ NEEFQVQQTL GYSYGGDINI SNGLSGGLNG SKSFSETINY KQESYRTTID
RKTNHKSIGW GVEAHKIMNN GWGPYGRDSY DPTYGNELFL GGRQSSSNAG QNFLPTHQMP
LLARGNFNPE FISVLSHKQN DTKKSKIKVT YQREMDRYTN QWNRLHWVGN NYKNQNTVTF
TSTYEVDWQN HTVKLIGTDS KETNPGV
