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STC2_STAAU
ID   STC2_STAAU              Reviewed;         715 AA.
AC   P17855;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 77.
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=BB;
RX   PubMed=3481366; DOI=10.1093/oxfordjournals.jbchem.a122156;
RA   Kaida S., Miyata T., Yoshizawa Y., Kawabata S., Morita T., Igarashi H.,
RA   Iwanaga S.;
RT   "Nucleotide sequence of the staphylocoagulase gene: its unique COOH-
RT   terminal 8 tandem repeats.";
RL   J. Biochem. 102:1177-1186(1987).
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; D00184; BAA00126.1; -; Genomic_DNA.
DR   PIR; A41511; A41511.
DR   PDB; 2A1D; X-ray; 3.50 A; D/H=27-355.
DR   PDBsum; 2A1D; -.
DR   AlphaFoldDB; P17855; -.
DR   SMR; P17855; -.
DR   EvolutionaryTrace; P17855; -.
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; 8.
DR   PROSITE; PS00429; STAPHYLOCOAGULASE; 8.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Prothrombin activator; Repeat;
KW   Signal.
FT   SIGNAL          1..26
FT   CHAIN           27..715
FT                   /note="Staphylocoagulase"
FT                   /id="PRO_0000022425"
FT   REPEAT          495..521
FT                   /note="1"
FT   REPEAT          522..548
FT                   /note="2"
FT   REPEAT          549..575
FT                   /note="3"
FT   REPEAT          576..602
FT                   /note="4"
FT   REPEAT          603..629
FT                   /note="5"
FT   REPEAT          630..656
FT                   /note="6"
FT   REPEAT          657..683
FT                   /note="7"
FT   REPEAT          684..710
FT                   /note="8"
FT   REGION          306..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..710
FT                   /note="8 X 27 AA tandem repeats of A-R-P-[RT]-[FQY]-[NK]-K-
FT                   [PA]-S-[EK]-T-N-A-Y-N-V-T-T-[NH]-[QAG]-[DN]-G-[TQ]-[VA]-
FT                   [ST]-Y-G"
FT   REGION          674..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            41..44
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           50..72
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           82..118
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           142..168
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           178..203
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   TURN            206..208
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           209..223
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           235..256
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           278..294
FT                   /evidence="ECO:0007829|PDB:2A1D"
FT   HELIX           299..301
FT                   /evidence="ECO:0007829|PDB:2A1D"
SQ   SEQUENCE   715 AA;  80100 MW;  46ABC9567AF5F128 CRC64;
     MKKQIISLGA LAVASSLFTW DNKADAIVTK DYSKESRVNE NSKYGTLISD WYLKGRLTSL
     ESQFINALDI LETYHYGEKE YKDAKDKLMT RILGEDQYLL ERKKVQYEEY KKLYQKYKEE
     NPTSKGLKLK TFDQYTIEDL TMREYNELTE SLKSAVKDFE KDVEKIENQH HDLKPFTDEM
     EEKATSRVDD LANKAYSVYF AFVRDTQHKT EALELKAKVD LVLGDEDKPH RISNERIEKE
     MIKDLESIIE DFFIETGLNK PGNITSYDSS KHHYKNHSEG FEALVKETRE AVANADESWK
     TKTVKKYGES ETKSPVVKEE NKVEDPQSPK FDNQQEVKTT AGKAEETTQP VAQPLVKIPQ
     GTITGEIVKG PEYPTMENKT LQGEIVQGPD FPTMEQSGPS LSDNYTQPTT PNPILEGLEG
     SSSKLEIKPQ GTESTLKGIQ GESSDIEVKP QATETTEASQ YGPRPQFNKT PKYVKYRDAG
     TGIREYNDGT FGYEARPRFN KPSETNAYNV TTNQDGTVSY GARPTQNKAS ETNAYNVTTH
     ANGQVSYGAR PTQKKPSETN AYNVTTHANG QVSYGARPTY NKPSETNAYN VTTHGNGQVS
     YGARPTYKKP SKTNAYNVTT HANGQVSYGA RPTQNKPSET NAYNVTTHAN GQVSYGARPT
     QNKPSETNAY NVTTHGNGQV SYGARPTYNK PSKTNAYNVT THADGTATYG PRVTK
 
 
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