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 27-MAR-2024, entry version 138.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; 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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 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 NCBIfam; NF035945; Zn_serralysin; 1.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
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 PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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
//
