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 11-MAY-2016, entry version 116. 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; Enterobacteriales; OC Enterobacteriaceae; 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; 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 RT residues in the middle region containing the sole methionine residue, RT and a probable 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 RT from 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 CC the emerging moth to dissolve its cocoon. CC -!- CATALYTIC ACTIVITY: Preferential cleavage of bonds with CC hydrophobic residues in P1'. 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 CC strain presents in the gut of silkworms, is used as a food CC supplement because it is reported to induces fibrinolytic, anti- CC inflammatory and anti-edemic (prevents swelling and fluid CC retention) activity in a number of tissues. CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 hemolysin-type calcium-binding repeats. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA27738.1; Type=Frameshift; Positions=350, 355; 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 ProteinModelPortal; P07268; -. DR SMR; P07268; 20-487. 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 Gene3D; 2.150.10.10; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR001818; Pept_M10_metallopeptidase. DR InterPro; IPR016294; Pept_M10B. DR InterPro; IPR013858; Peptidase_M10B_C. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. 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; KW Metal-binding; Metalloprotease; Protease; Repeat; Secreted; Zinc; KW Zymogen. FT PROPEP 1 16 {ECO:0000269|PubMed:6396298}. FT /FTId=PRO_0000028695. FT CHAIN 17 487 Serralysin. FT /FTId=PRO_0000028696. FT REPEAT 348 365 Hemolysin-type calcium-binding 1. FT REPEAT 366 383 Hemolysin-type calcium-binding 2. FT ACT_SITE 193 193 FT METAL 192 192 Zinc; catalytic. FT METAL 196 196 Zinc; catalytic. FT METAL 202 202 Zinc; catalytic. FT METAL 232 232 Zinc; catalytic. FT METAL 269 269 Calcium 1; via carbonyl oxygen. FT METAL 271 271 Calcium 1; via carbonyl oxygen. FT METAL 273 273 Calcium 1. FT METAL 301 301 Calcium 1. FT METAL 303 303 Calcium 1; via carbonyl oxygen. FT METAL 304 304 Calcium 2; via carbonyl oxygen. FT METAL 306 306 Calcium 1. FT METAL 306 306 Calcium 2. FT METAL 343 343 Calcium 2; via carbonyl oxygen. FT METAL 345 345 Calcium 2. FT METAL 350 350 Calcium 3; via carbonyl oxygen. FT METAL 352 352 Calcium 3; via carbonyl oxygen. FT METAL 354 354 Calcium 3. FT METAL 359 359 Calcium 4; via carbonyl oxygen. FT METAL 361 361 Calcium 4; via carbonyl oxygen. FT METAL 363 363 Calcium 4. FT METAL 367 367 Calcium 3; via carbonyl oxygen. FT METAL 368 368 Calcium 5; via carbonyl oxygen. FT METAL 369 369 Calcium 3; via carbonyl oxygen. FT METAL 372 372 Calcium 3. FT METAL 372 372 Calcium 5. FT METAL 376 376 Calcium 4; via carbonyl oxygen. FT METAL 377 377 Calcium 6; via carbonyl oxygen. FT METAL 378 378 Calcium 4; via carbonyl oxygen. FT METAL 379 379 Calcium 6; via carbonyl oxygen. FT METAL 381 381 Calcium 4. FT METAL 381 381 Calcium 6. FT METAL 385 385 Calcium 5; via carbonyl oxygen. FT METAL 386 386 Calcium 7; via carbonyl oxygen. FT METAL 387 387 Calcium 5; via carbonyl oxygen. FT METAL 388 388 Calcium 7; via carbonyl oxygen. FT METAL 390 390 Calcium 5. FT METAL 390 390 Calcium 7. FT METAL 399 399 Calcium 6. FT METAL 406 406 Calcium 6. FT METAL 416 416 Calcium 7. FT HELIX 21 29 {ECO:0000244|PDB:1SRP}. FT TURN 30 32 {ECO:0000244|PDB:1SRP}. FT STRAND 39 44 {ECO:0000244|PDB:1SRP}. FT HELIX 48 55 {ECO:0000244|PDB:1SRP}. FT TURN 56 58 {ECO:0000244|PDB:1SRP}. FT STRAND 72 77 {ECO:0000244|PDB:1SRP}. FT HELIX 99 115 {ECO:0000244|PDB:1SRP}. FT STRAND 116 122 {ECO:0000244|PDB:1SRP}. FT STRAND 125 127 {ECO:0000244|PDB:1SRP}. FT STRAND 130 136 {ECO:0000244|PDB:1SRP}. FT STRAND 138 140 {ECO:0000244|PDB:1SRP}. FT STRAND 150 152 {ECO:0000244|PDB:1SRP}. FT STRAND 167 171 {ECO:0000244|PDB:1SRP}. FT HELIX 175 178 {ECO:0000244|PDB:1SRP}. FT TURN 180 182 {ECO:0000244|PDB:1SRP}. FT HELIX 184 197 {ECO:0000244|PDB:1SRP}. FT STRAND 208 211 {ECO:0000244|PDB:1SRP}. FT HELIX 215 217 {ECO:0000244|PDB:1SRP}. FT TURN 225 227 {ECO:0000244|PDB:1SRP}. FT HELIX 235 238 {ECO:0000244|PDB:1SRP}. FT HELIX 252 262 {ECO:0000244|PDB:1SRP}. FT TURN 266 269 {ECO:0000244|PDB:1SRP}. FT STRAND 274 276 {ECO:0000244|PDB:1SRP}. FT HELIX 284 286 {ECO:0000244|PDB:1SRP}. FT STRAND 297 299 {ECO:0000244|PDB:1SRP}. FT STRAND 307 309 {ECO:0000244|PDB:1SRP}. FT STRAND 318 320 {ECO:0000244|PDB:1SRP}. FT STRAND 326 328 {ECO:0000244|PDB:1SRP}. FT STRAND 336 338 {ECO:0000244|PDB:1SRP}. FT STRAND 346 348 {ECO:0000244|PDB:1SRP}. FT STRAND 355 357 {ECO:0000244|PDB:1SRP}. FT STRAND 364 366 {ECO:0000244|PDB:1SRP}. FT STRAND 373 375 {ECO:0000244|PDB:1SRP}. FT STRAND 382 384 {ECO:0000244|PDB:1SRP}. FT STRAND 391 393 {ECO:0000244|PDB:1SRP}. FT HELIX 397 400 {ECO:0000244|PDB:1SRP}. FT STRAND 406 410 {ECO:0000244|PDB:1SRP}. FT TURN 413 415 {ECO:0000244|PDB:1SRP}. FT STRAND 416 419 {ECO:0000244|PDB:1SRP}. FT HELIX 421 427 {ECO:0000244|PDB:1SRP}. FT STRAND 432 435 {ECO:0000244|PDB:1SRP}. FT STRAND 445 451 {ECO:0000244|PDB:1SRP}. FT TURN 452 455 {ECO:0000244|PDB:1SRP}. FT STRAND 456 461 {ECO:0000244|PDB:1SRP}. FT STRAND 470 477 {ECO:0000244|PDB:1SRP}. FT TURN 481 483 {ECO:0000244|PDB:1SRP}. FT STRAND 484 486 {ECO:0000244|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 //