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 25-MAY-2022, entry version 132. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 METAL 192 FT /note="Zinc; catalytic" FT METAL 196 FT /note="Zinc; catalytic" FT METAL 202 FT /note="Zinc; catalytic" FT METAL 232 FT /note="Zinc; catalytic" FT METAL 269 FT /note="Calcium 1; via carbonyl oxygen" FT METAL 271 FT /note="Calcium 1; via carbonyl oxygen" FT METAL 273 FT /note="Calcium 1" FT METAL 301 FT /note="Calcium 1" FT METAL 303 FT /note="Calcium 1; via carbonyl oxygen" FT METAL 304 FT /note="Calcium 2; via carbonyl oxygen" FT METAL 306 FT /note="Calcium 1" FT METAL 306 FT /note="Calcium 2" FT METAL 343 FT /note="Calcium 2; via carbonyl oxygen" FT METAL 345 FT /note="Calcium 2" FT METAL 350 FT /note="Calcium 3; via carbonyl oxygen" FT METAL 352 FT /note="Calcium 3; via carbonyl oxygen" FT METAL 354 FT /note="Calcium 3" FT METAL 359 FT /note="Calcium 4; via carbonyl oxygen" FT METAL 361 FT /note="Calcium 4; via carbonyl oxygen" FT METAL 363 FT /note="Calcium 4" FT METAL 367 FT /note="Calcium 3; via carbonyl oxygen" FT METAL 368 FT /note="Calcium 5; via carbonyl oxygen" FT METAL 369 FT /note="Calcium 3; via carbonyl oxygen" FT METAL 372 FT /note="Calcium 3" FT METAL 372 FT /note="Calcium 5" FT METAL 376 FT /note="Calcium 4; via carbonyl oxygen" FT METAL 377 FT /note="Calcium 6; via carbonyl oxygen" FT METAL 378 FT /note="Calcium 4; via carbonyl oxygen" FT METAL 379 FT /note="Calcium 6; via carbonyl oxygen" FT METAL 381 FT /note="Calcium 4" FT METAL 381 FT /note="Calcium 6" FT METAL 385 FT /note="Calcium 5; via carbonyl oxygen" FT METAL 386 FT /note="Calcium 7; via carbonyl oxygen" FT METAL 387 FT /note="Calcium 5; via carbonyl oxygen" FT METAL 388 FT /note="Calcium 7; via carbonyl oxygen" FT METAL 390 FT /note="Calcium 5" FT METAL 390 FT /note="Calcium 7" FT METAL 399 FT /note="Calcium 6" FT METAL 406 FT /note="Calcium 6" FT METAL 416 FT /note="Calcium 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 //