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PRZN_SERME
ID   PRZN_SERME              Reviewed;         487 AA.
AC   P07268;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Serralysin;
DE            EC=3.4.24.40;
DE   AltName: Full=Extracellular metalloproteinase;
DE   AltName: Full=Serratiopeptidase;
DE            Short=Serrapeptase;
DE            Short=Serrapeptidase;
DE   AltName: Full=Zinc proteinase;
DE   Flags: Precursor;
OS   Serratia marcescens (strain ATCC 21074 / E-15).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; unclassified Serratia.
OX   NCBI_TaxID=617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3016665; DOI=10.1093/nar/14.14.5843;
RA   Nakahama K., Yoshimura K., Marumoto R., Kikuchi M., Lee I.S., Hase T.,
RA   Matsubara H.;
RT   "Cloning and sequencing of Serratia protease gene.";
RL   Nucleic Acids Res. 14:5843-5855(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-34 AND 179-269.
RX   PubMed=6396298; DOI=10.1093/oxfordjournals.jbchem.a134969;
RA   Lee I.S., Wakabayashi S., Miyata K., Tomoda K., Yoneda M., Kangawa K.,
RA   Minamino N., Matsuo H., Matsubara H.;
RT   "Serratia protease. Amino acid sequences of both termini, the 53 residues
RT   in the middle region containing the sole methionine residue, and a probable
RT   zinc-binding region.";
RL   J. Biochem. 96:1409-1418(1984).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-487.
RX   PubMed=8797082; DOI=10.1093/oxfordjournals.jbchem.a021320;
RA   Hamada K., Hata Y., Katsuya Y., Hiramatsu H., Fujiwara T., Katsube Y.;
RT   "Crystal structure of Serratia protease, a zinc-dependent proteinase from
RT   Serratia sp. E-15, containing a beta-sheet coil motif at 2.0-A
RT   resolution.";
RL   J. Biochem. 119:844-851(1996).
CC   -!- FUNCTION: Naturally present in the silkworm intestine and allows the
CC       emerging moth to dissolve its cocoon.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'.; EC=3.4.24.40;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 7 Ca(2+) ions per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: The Gly-rich repeats may be important in the
CC       extracellular secretion of this metalloprotease.
CC   -!- MISCELLANEOUS: In Japan this enzyme, isolated from a Serratia strain
CC       presents in the gut of silkworms, is used as a food supplement because
CC       it is reported to induces fibrinolytic, anti-inflammatory and anti-
CC       edemic (prevents swelling and fluid retention) activity in a number of
CC       tissues.
CC   -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA27738.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X04127; CAA27738.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A23596; HYSE15.
DR   PDB; 1SRP; X-ray; 2.00 A; A=17-487.
DR   PDBsum; 1SRP; -.
DR   AlphaFoldDB; P07268; -.
DR   SMR; P07268; -.
DR   MEROPS; M10.051; -.
DR   EvolutionaryTrace; P07268; -.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IMP:CACAO.
DR   CDD; cd04277; ZnMc_serralysin_like; 1.
DR   Gene3D; 2.150.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR016294; Pept_M10B.
DR   InterPro; IPR013858; Peptidase_M10B_C.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR034033; Serralysin-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF00353; HemolysinCabind; 1.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   Pfam; PF08548; Peptidase_M10_C; 1.
DR   PIRSF; PIRSF001205; Peptidase_M10B; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF51120; SSF51120; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Repeat; Secreted; Zinc; Zymogen.
FT   PROPEP          1..16
FT                   /evidence="ECO:0000269|PubMed:6396298"
FT                   /id="PRO_0000028695"
FT   CHAIN           17..487
FT                   /note="Serralysin"
FT                   /id="PRO_0000028696"
FT   REPEAT          348..365
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          366..383
FT                   /note="Hemolysin-type calcium-binding 2"
FT   ACT_SITE        193
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         303
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         343
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         361
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         363
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         367
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         368
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT   BINDING         369
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         372
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         372
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT   BINDING         376
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         377
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT   BINDING         378
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         379
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT   BINDING         381
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT   BINDING         381
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT   BINDING         385
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT   BINDING         386
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT   BINDING         387
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT   BINDING         399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT   BINDING         406
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT   BINDING         416
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           48..55
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           99..115
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           184..197
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          208..211
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           215..217
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           252..262
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            266..269
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           284..286
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          318..320
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          355..357
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          382..384
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          406..410
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            413..415
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          416..419
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   HELIX           421..427
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          432..435
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          445..451
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            452..455
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          456..461
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          470..477
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:1SRP"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:1SRP"
SQ   SEQUENCE   487 AA;  52235 MW;  270A315CADD568C3 CRC64;
     MQSTKKAIEI TESNFAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ AGLFITRENQ
     TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE QQQQAKLSLQ SWADVANITF
     TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP
     ATEDYGRQTF THEIGHALGL SHPGDYNAGE GNPTYRDVTY AEDTRQFSLM SYWSETNTGG
     DNGGHYAAAP LLDDIAAIQH LYGANLSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW
     DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG SGNDVIVGNA
     ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS APGASDWIRD FQKGIDKIDL
     SFFNKEAQSS DFIHFVDHFS GAAGEALLSY NASNNVTDLS VNIGGHQAPD FLVKIVGQVD
     VATDFIV
 
 
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