ID PRZN_SERSP STANDARD; PRT; 486 AA. AC P07268; DT 01-APR-1988 (REL. 07, CREATED) DT 01-APR-1988 (REL. 07, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, 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; GAMMA SUBDIVISION; ENTEROBACTERIACEAE; OC SERRATIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 86286592. 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. 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). RX MEDLINE; 96389988. 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 AND REQUIRES A ZINC ATOM, WHICH IS ESSENTIAL FOR CC PROTEOLYTIC ACTIVITY. CC -!- SUBCELLULAR LOCATION: SECRETED. CC -!- THE GLY-RICH REPEATS MAY BE IMPORTANT IN THE EXTRACELLULAR CC SECRETION OF THIS METALLOPROTEASE. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M10B (ZINC CC METALLOPROTEASE); ALSO KNOWN AS THE SERRALYSIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G47591; -. DR PIR; A23596; HYSE15. DR PDB; 1SRP; 14-FEB-95. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1. DR PFAM; PF00099; zn-protease; 1. DR PFAM; PF00353; hemolysinCabind; 1. KW HYDROLASE; ZINC; METALLOPROTEASE; ZYMOGEN; CALCIUM; REPEAT; KW 3D-STRUCTURE. FT PROPEP 1 16 FT CHAIN 17 486 SERRALYSIN. 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 DOMAIN 366 389 3 X REPEATS, GLY-RICH. FT REPEAT 366 371 1. FT REPEAT 375 380 2. FT REPEAT 384 389 3. SQ SEQUENCE 486 AA; 52406 MW; 72AF33D0 CRC32; 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 GVTIENAIGF RQRLIVGNAA NNVLKGGAGN DVLFGGGGAD ELWGGAGKDI FVFSAASDSA PGASDWIRDF QKGIDKIDLS FFNKEAQSSD FIHFVDHFSG AAGEALLSYN ASNNVTDLSV NIGGHQAPDF LVKIVGQVDV ATDFIV //