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-APR-2013, entry version 107. 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; 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: Binds 7 calcium ions per subunit. CC -!- COFACTOR: 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. CC -!- SIMILARITY: Contains 2 hemolysin-type calcium-binding repeats. CC -!- SEQUENCE CAUTION: CC Sequence=CAA27738.1; Type=Frameshift; Positions=350, 355; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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. 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; PF00353; HemolysinCabind; 4. 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; Serralysn_like_C; 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 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 FT TURN 30 32 FT STRAND 39 44 FT HELIX 48 55 FT TURN 56 58 FT STRAND 72 77 FT HELIX 99 115 FT STRAND 116 122 FT STRAND 125 127 FT STRAND 130 136 FT STRAND 138 140 FT STRAND 150 152 FT STRAND 167 171 FT HELIX 175 178 FT TURN 180 182 FT HELIX 184 197 FT STRAND 208 211 FT HELIX 215 217 FT TURN 225 227 FT HELIX 235 238 FT HELIX 252 262 FT TURN 266 269 FT STRAND 274 276 FT HELIX 284 286 FT STRAND 297 299 FT STRAND 307 309 FT STRAND 318 320 FT STRAND 326 328 FT STRAND 336 338 FT STRAND 346 348 FT STRAND 355 357 FT STRAND 364 366 FT STRAND 373 375 FT STRAND 382 384 FT STRAND 391 393 FT HELIX 397 400 FT STRAND 406 410 FT TURN 413 415 FT STRAND 416 419 FT HELIX 421 427 FT STRAND 432 435 FT STRAND 445 451 FT TURN 452 455 FT STRAND 456 461 FT STRAND 470 477 FT TURN 481 483 FT STRAND 484 486 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 //