ID   STC1_STAAU              Reviewed;         658 AA.
AC   P07767;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Staphylocoagulase;
DE   Flags: Precursor;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=213;
RX   PubMed=2587230; DOI=10.1093/nar/17.21.8871;
RA   Kaida S., Miyata T., Yoshizawa Y., Igarashi H., Iwanaga S.;
RT   "Nucleotide and deduced amino acid sequences of staphylocoagulase gene from
RT   Staphylococcus aureus strain 213.";
RL   Nucleic Acids Res. 17:8871-8871(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-350.
RC   STRAIN=213;
RX   PubMed=3941089; DOI=10.1016/s0021-9258(17)36123-9;
RA   Kawabata S., Miyata T., Morita T., Miyata T., Iwanaga S., Igarashi H.;
RT   "The amino acid sequence of the procoagulant- and prothrombin-binding
RT   domain isolated from staphylocoagulase.";
RL   J. Biol. Chem. 261:527-531(1986).
CC   -!- FUNCTION: Staphylocoagulase is an extracellular protein which
CC       specifically forms a complex with human prothrombin. This complex named
CC       staphylothrombin can clot fibrinogen without any proteolytic cleavage
CC       of prothrombin.
CC   -!- DOMAIN: The C-terminal tandem repeats are not required for the
CC       procoagulant activity.
CC   -!- SIMILARITY: Belongs to the staphylocoagulase family. {ECO:0000305}.
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DR   EMBL; X16457; CAA34476.1; -; Genomic_DNA.
DR   PIR; S06744; S06744.
DR   AlphaFoldDB; P07767; -.
DR   SMR; P07767; -.
DR   PRO; PR:P07767; -.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.750; -; 1.
DR   Gene3D; 1.20.120.760; -; 1.
DR   InterPro; IPR043072; Staphylcoagulase_N_1.
DR   InterPro; IPR043071; Staphylcoagulase_N_2.
DR   InterPro; IPR001443; Staphylcoagulase_rpt.
DR   InterPro; IPR014874; Staphylocoagulase_N.
DR   Pfam; PF08764; Coagulase; 1.
DR   Pfam; PF04022; Staphylcoagulse; 6.
DR   PROSITE; PS00429; STAPHYLOCOAGULASE; 6.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Prothrombin activator; Repeat; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:3941089"
FT   CHAIN           27..658
FT                   /note="Staphylocoagulase"
FT                   /id="PRO_0000022424"
FT   REPEAT          492..518
FT                   /note="1"
FT   REPEAT          519..545
FT                   /note="2"
FT   REPEAT          546..572
FT                   /note="3"
FT   REPEAT          573..599
FT                   /note="4"
FT   REPEAT          600..626
FT                   /note="5"
FT   REPEAT          627..653
FT                   /note="6"
FT   REGION          391..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..653
FT                   /note="6 X 27 AA tandem repeats of A-R-P-[RT]-[FQY]-[NK]-K-
FT                   P-S-[EK]-T-N-A-Y-N-V-T-T-[NH]-[QA]-[DN]-G-[TQ]-[VA]-[ST]-Y-
FT                   G"
FT   REGION          619..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        350
FT                   /note="Q -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   658 AA;  74505 MW;  54B58769C25450B4 CRC64;
     MKKQIISLGA LAVASSLFTW DNKADAIVTK DYSKESRVNE KSKKGATVSD YYYWKIIDSL
     EAQFTGAIDL LENYKYGDPI YKEAKDRLMT RVLGEDQYLL KKKIDEYELY KKWYKSSNKN
     TNMLTFHKYN LYNLTMNEYN DIFNSLKDAV YQFNKEVKEI EHKNVDLKQF DKDGEDKATK
     EVYDLVSEID TLVVTYYADK DYGEHAKELR AKLDLILGDT DNPHKITNER IKKEMIDDLN
     SIIDDFFMET KQNRPNSITK YDPTKHNFKE KSENKPNFDK LVEETKKAVK EADESWKNKT
     VKKYEETVTK SPVVKEEKKV EEPQLPKVGN QQEVKTTAGK AEETTQPVAQ PLVKIPQETI
     YGETVKGPEY PTMENKTLQG EIVQGPDFLT MEQNRPSLSD NYTQPTTPNP ILEGLEGSSS
     KLEIKPQGTE STLKGIQGES SDIEVKPQAT ETTEASQYGP RPQFNKTPKY VKYRDAGTGI
     REYNDGTFGY EARPRFNKPS ETNAYNVTTN QDGTVSYGAR PTQNKPSETN AYNVTTHANG
     QVSYGARPTQ NKPSKTNAYN VTTHANGQVS YGARPTQKKP SKTNAYNVTT HANGQVSYGA
     RPTYKKPSET NAYNVTTHAN GQVSYGARPT QKKPSETNAY NVTTHADGTA TYGPRVTK