ID PRZN_SERSP STANDARD; PRT; 487 AA. AC P07268; DT 01-APR-1988 (Rel. 07, Created) DT 15-SEP-2003 (Rel. 42, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Serralysin precursor (EC 3.4.24.40) (Extracellular metalloproteinase) DE (Zinc proteinase). OS Serratia sp. (strain E-15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=617; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86286592; PubMed=3016665; RA Nakahama K., Yoshimura K., Marumoto R., Kikuchi M., Lee I.S., RA Hase T., Matsubara H.; RT "Cloning and sequencing of Serratia protease gene."; RL Nucleic Acids Res. 14:5843-5855(1986). RN [2] RP SEQUENCE OF 17-34 AND 179-269. RX MEDLINE=85130873; 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 CONCEPTUAL TRANSLATION. RA Axelsen K.B.; RL Unpublished observations (MAY-2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=96389988; 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 -!- CATALYTIC ACTIVITY: Preferential cleavage of bonds with CC hydrophobic residues in P1'. CC -!- COFACTOR: Binds 1 zinc ion and 7 calcium ions per subunit. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- MISCELLANEOUS: THE GLY-RICH REPEATS MAY BE IMPORTANT IN THE CC EXTRACELLULAR SECRETION OF THIS METALLOPROTEASE. CC -!- SIMILARITY: Belongs to peptidase family M10B. CC -!- CAUTION: Ref.1 sequence differs from that shown due to CC frameshifts in positions 350 and 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. DR PIR; A23596; HYSE15. DR PDB; 1SRP; 14-FEB-95. DR MEROPS; M10.051; -. DR InterPro; IPR001343; Hemlysn_Ca_bind. DR InterPro; IPR006026; NZn_MTpeptdse. DR InterPro; IPR006025; Zn_MTpeptdse_BS. DR Pfam; PF00353; hemolysinCabind; 2. DR PRINTS; PR00313; CABNDNGRPT. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1. KW Hydrolase; Metalloprotease; Calcium-binding; Metal-binding; Zinc; KW Repeat; Zymogen; 3D-structure. FT PROPEP 1 16 FT CHAIN 17 487 SERRALYSIN. FT REPEAT 349 357 GGXGXD 1. FT REPEAT 358 366 GGXGXD 2. FT REPEAT 367 375 GGXGXD 3. FT REPEAT 376 384 GGXGXD 4. FT REPEAT 385 393 GGXGXD 5. FT METAL 192 192 ZINC (CATALYTIC). FT ACT_SITE 193 193 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 AND 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 AND 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 AND 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 AND 7. FT METAL 399 399 CALCIUM 6. FT METAL 406 406 CALCIUM 6. FT METAL 416 416 CALCIUM 7. SQ SEQUENCE 487 AA; 52234 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 //