STRP_STREQ
ID STRP_STREQ Reviewed; 440 AA.
AC P00779;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Streptokinase C;
DE Flags: Precursor;
GN Name=skc;
OS Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=119602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H46A;
RX PubMed=2989113; DOI=10.1016/0378-1119(85)90145-3;
RA Malke H., Roe B.A., Ferretti J.J.;
RT "Nucleotide sequence of the streptokinase gene from Streptococcus
RT equisimilis H46A.";
RL Gene 34:357-362(1985).
RN [2]
RP PROTEIN SEQUENCE OF 27-440.
RX PubMed=6760891; DOI=10.1021/bi00269a001;
RA Jackson K.W., Tang J.;
RT "Complete amino acid sequence of streptokinase and its homology with serine
RT proteases.";
RL Biochemistry 21:6620-6625(1982).
CC -!- FUNCTION: This protein is not a protease, but it activates plasminogen
CC by complexing with it. As a potential virulence factor, it is thought
CC to prevent the formation of effective fibrin barriers around the site
CC of infection, thereby contributing to the invasiveness of the cells.
CC -!- INTERACTION:
CC P00779; P00747: PLG; Xeno; NbExp=2; IntAct=EBI-1035089, EBI-999394;
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DR EMBL; K02986; AAA26974.1; -; Genomic_DNA.
DR EMBL; X72832; CAA51351.1; -; Genomic_DNA.
DR PIR; A00967; BZSO.
DR PIR; A22801; A22801.
DR PDB; 1BML; X-ray; 2.90 A; C/D=38-398.
DR PDB; 1L4D; X-ray; 2.30 A; B=40-173.
DR PDB; 1L4Z; X-ray; 2.80 A; B=27-173.
DR PDB; 1QQR; X-ray; 2.30 A; A/B/C/D=177-314.
DR PDBsum; 1BML; -.
DR PDBsum; 1L4D; -.
DR PDBsum; 1L4Z; -.
DR PDBsum; 1QQR; -.
DR AlphaFoldDB; P00779; -.
DR SMR; P00779; -.
DR IntAct; P00779; 1.
DR EvolutionaryTrace; P00779; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR InterPro; IPR036120; SAK/SK_sf.
DR InterPro; IPR008124; SK.
DR PRINTS; PR01753; STREPKINASE.
DR SUPFAM; SSF54328; SSF54328; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Plasminogen activation; Signal;
KW Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:6760891"
FT CHAIN 27..440
FT /note="Streptokinase C"
FT /id="PRO_0000022428"
FT VARIANT 195
FT /note="L -> D"
FT VARIANT 207
FT /note="D -> L"
FT CONFLICT 298..300
FT /note="EKY -> LEYK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1L4Z"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:1L4D"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1L4Z"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1L4Z"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1L4D"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:1L4D"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1BML"
FT STRAND 184..196
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1QQR"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 240..252
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1QQR"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 292..304
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1QQR"
FT STRAND 316..327
FT /evidence="ECO:0007829|PDB:1BML"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1BML"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:1BML"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1BML"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:1BML"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1BML"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:1BML"
FT STRAND 386..397
FT /evidence="ECO:0007829|PDB:1BML"
SQ SEQUENCE 440 AA; 50140 MW; 8FC1F22648ACC77A CRC64;
MKNYLSFGMF ALLFALTFGT VNSVQAIAGP EWLLDRPSVN NSQLVVSVAG TVEGTNQDIS
LKFFEIDLTS RPAHGGKTEQ GLSPKSKPFA TDSGAMSHKL EKADLLKAIQ EQLIANVHSN
DDYFEVIDFA SDATITDRNG KVYFADKDGS VTLPTQPVQE FLLSGHVRVR PYKEKPIQNQ
AKSVDVEYTV QFTPLNPDDD FRPGLKDTKL LKTLAIGDTI TSQELLAQAQ SILNKNHPGY
TIYERDSSIV THDNDIFRTI LPMDQEFTYR VKNREQAYRI NKKSGLNEEI NNTDLISEKY
YVLKKGEKPY DPFDRSHLKL FTIKYVDVDT NELLKSEQLL TASERNLDFR DLYDPRDKAK
LLYNNLDAFG IMDYTLTGKV EDNHDDTNRI ITVYMGKRPE GENASYHLAY DKDRYTEEER
EVYSYLRYTG TPIPDNPNDK
