ID PRZN_SERSP STANDARD; PRT; 487 AA. AC P07268; DT 01-APR-1988 (Rel. 07, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 01-MAY-2005 (Rel. 47, 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 NUCLEOTIDE SEQUENCE. RX MEDLINE=86286592; PubMed=3016665; 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 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 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 the peptidase M10B family. CC -!- CAUTION: This is a conceptual translation. CC -!- CAUTION: Ref.1 sequence differs from that shown due to frameshifts CC 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; X-ray; @=17-486. DR SMR; P07268; 20-487. DR MEROPS; M10.051; -. DR InterPro; IPR001343; Hemlysn_Ca_bind. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR006026; Peptidase_M. DR InterPro; IPR011049; Serralysn_like_C. DR Pfam; PF00353; HemolysinCabind; 2. DR PRINTS; PR00313; CABNDNGRPT. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW 3D-structure; Calcium-binding; Direct protein sequencing; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Repeat; Zinc; Zymogen. 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. FT HELIX 21 29 FT TURN 30 32 FT TURN 36 37 FT STRAND 39 39 FT STRAND 44 44 FT HELIX 48 55 FT TURN 56 58 FT TURN 62 63 FT TURN 65 66 FT STRAND 72 77 FT TURN 83 84 FT TURN 88 89 FT STRAND 92 92 FT STRAND 95 95 FT HELIX 99 115 FT STRAND 116 116 FT STRAND 118 122 FT STRAND 131 136 FT STRAND 138 140 FT TURN 141 142 FT STRAND 143 144 FT STRAND 150 152 FT STRAND 158 159 FT TURN 160 161 FT STRAND 162 163 FT TURN 165 166 FT STRAND 167 171 FT TURN 172 173 FT HELIX 175 178 FT TURN 180 182 FT HELIX 184 198 FT TURN 199 199 FT HELIX 215 217 FT STRAND 220 220 FT TURN 221 222 FT TURN 225 227 FT TURN 229 230 FT HELIX 235 238 FT TURN 239 239 FT STRAND 241 241 FT TURN 243 244 FT HELIX 252 262 FT STRAND 264 264 FT TURN 266 269 FT STRAND 274 276 FT TURN 277 278 FT HELIX 284 286 FT STRAND 287 287 FT TURN 291 292 FT STRAND 297 299 FT STRAND 307 309 FT TURN 311 312 FT STRAND 318 320 FT TURN 323 324 FT STRAND 326 328 FT TURN 330 331 FT STRAND 333 333 FT STRAND 336 338 FT TURN 340 341 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 401 401 FT TURN 402 403 FT STRAND 404 404 FT STRAND 406 408 FT TURN 413 415 FT STRAND 417 419 FT HELIX 421 427 FT TURN 428 428 FT TURN 430 431 FT STRAND 434 435 FT TURN 443 444 FT STRAND 445 451 FT TURN 452 455 FT STRAND 456 461 FT STRAND 471 476 FT TURN 481 483 FT STRAND 485 487 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 //