ID   SAK_STAAU               Reviewed;         163 AA.
AC   P68802; P00802;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Staphylokinase;
DE   AltName: Full=Neutral proteinase;
DE   AltName: Full=Protease III;
DE   AltName: Full=SakSTAR;
DE   Flags: Precursor;
GN   Name=sak;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6359061; DOI=10.1093/nar/11.22.7679;
RA   Sako T., Tsuchida N.;
RT   "Nucleotide sequence of the staphylokinase gene from Staphylococcus
RT   aureus.";
RL   Nucleic Acids Res. 11:7679-7693(1983).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 43-163.
RX   PubMed=9145104; DOI=10.1038/nsb0597-357;
RA   Rabijns A., de Bondt H.L., de Ranter C.;
RT   "Three-dimensional structure of staphylokinase, a plasminogen activator
RT   with therapeutic potential.";
RL   Nat. Struct. Biol. 4:357-360(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 36-163 IN COMPLEX IN PLASMINOGEN.
RX   PubMed=9783753; DOI=10.1038/2359;
RA   Parry M.A., Fernandez-Catalan C., Bergner A., Huber R., Hopfner K.P.,
RA   Schlott B., Guehrs K.H., Bode W.;
RT   "The ternary microplasmin-staphylokinase-microplasmin complex is a
RT   proteinase-cofactor-substrate complex in action.";
RL   Nat. Struct. Biol. 5:917-923(1998).
RN   [4]
RP   STRUCTURE BY NMR OF 28-163.
RX   PubMed=9692953; DOI=10.1021/bi980673i;
RA   Ohlenschlaeger O., Ramachandran R., Guehrs K.H., Schlott B., Brown L.R.;
RT   "Nuclear magnetic resonance solution structure of the plasminogen-activator
RT   protein staphylokinase.";
RL   Biochemistry 37:10635-10642(1998).
CC   -!- FUNCTION: Potent plasminogen activator that converts plasminogen into
CC       plasmin. It forms a 1:1 complex with plasmin, which in turn activates
CC       other plasminogen molecules.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PHARMACEUTICAL: Currently in clinical testing as a highly fibrin-
CC       specific thrombolytic agent for the treatment of patients with acute
CC       myocardial infarction or peripheral arterial occlusions.
CC   -!- SIMILARITY: Belongs to the staphylokinase family. {ECO:0000305}.
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DR   EMBL; X00127; CAA24957.1; -; Genomic_DNA.
DR   RefSeq; WP_000920038.1; NZ_WTUM01000080.1.
DR   PDB; 1C76; X-ray; 2.25 A; A=28-163.
DR   PDB; 1C77; X-ray; 2.30 A; A/B=28-163.
DR   PDB; 1C78; X-ray; 2.30 A; A/B=28-163.
DR   PDB; 1C79; X-ray; 2.30 A; A/B=28-163.
DR   PDB; 1SSN; NMR; -; A=28-163.
DR   PDB; 2SAK; X-ray; 1.80 A; A=43-163.
DR   PDBsum; 1C76; -.
DR   PDBsum; 1C77; -.
DR   PDBsum; 1C78; -.
DR   PDBsum; 1C79; -.
DR   PDBsum; 1SSN; -.
DR   PDBsum; 2SAK; -.
DR   AlphaFoldDB; P68802; -.
DR   BMRB; P68802; -.
DR   SMR; P68802; -.
DR   EvolutionaryTrace; P68802; -.
DR   PRO; PR:P68802; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR   InterPro; IPR004093; SAK.
DR   InterPro; IPR036120; SAK/SK_sf.
DR   Pfam; PF02821; Staphylokinase; 1.
DR   SUPFAM; SSF54328; SSF54328; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Pharmaceutical; Plasminogen activation; Secreted; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..163
FT                   /note="Staphylokinase"
FT                   /id="PRO_0000031603"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:1SSN"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1SSN"
FT   STRAND          51..59
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          65..75
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:1SSN"
FT   HELIX           84..95
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:2SAK"
FT   STRAND          151..161
FT                   /evidence="ECO:0007829|PDB:2SAK"
SQ   SEQUENCE   163 AA;  18490 MW;  E56D9FF50AEDE141 CRC64;
     MLKRSLLFLT VLLLLFSFSS ITNEVSASSS FDKGKYKKGD DASYFEPTGP YLMVNVTGVD
     GKGNELLSPH YVEFPIKPGT TLTKEKIEYY VEWALDATAY KEFRVVELDP SAKIEVTYYD
     KNKKKEETKS FPITEKGFVV PDLSEHIKNP GFNLITKVVI EKK