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 24-JAN-2006 (Rel. 49, 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 [GENOMIC DNA]. 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 7 calcium ions per subunit. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- SUBCELLULAR LOCATION: Secreted protein. 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; Genomic_DNA. DR PIR; A23596; HYSE15. DR PDB; 1SRP; X-ray; @=17-487. DR MEROPS; M10.051; -. DR LinkHub; P07268; -. DR InterPro; IPR001343; Hemlysn_Ca_bd. DR InterPro; IPR001818; Pept_M10A_M12B. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR006026; Peptidase_M. DR InterPro; IPR003995; RtxA. DR Pfam; PF00353; HemolysinCabind; 2. DR Pfam; PF00413; Peptidase_M10; 1. DR PRINTS; PR00313; CABNDNGRPT. DR PRINTS; PR01488; RTXTOXINA. DR SMART; SM00235; ZnMc; 1. DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Repeat; Zinc; Zymogen. FT PROPEP 1 16 FT /FTId=PRO_0000028695. FT CHAIN 17 487 Serralysin. FT /FTId=PRO_0000028696. 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 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 35 35 FT TURN 36 37 FT STRAND 39 44 FT HELIX 48 55 FT TURN 56 58 FT TURN 62 63 FT TURN 65 66 FT STRAND 69 69 FT STRAND 72 77 FT TURN 83 84 FT TURN 88 89 FT STRAND 90 90 FT STRAND 92 93 FT STRAND 95 95 FT HELIX 99 115 FT STRAND 116 122 FT STRAND 125 127 FT STRAND 130 136 FT STRAND 138 140 FT TURN 141 142 FT STRAND 143 144 FT STRAND 147 147 FT STRAND 150 152 FT STRAND 155 156 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 STRAND 174 174 FT HELIX 175 178 FT TURN 180 182 FT HELIX 184 197 FT TURN 198 199 FT STRAND 203 203 FT STRAND 208 211 FT HELIX 215 217 FT STRAND 219 220 FT TURN 221 222 FT STRAND 224 224 FT TURN 225 227 FT TURN 229 230 FT STRAND 233 233 FT HELIX 235 238 FT TURN 239 239 FT STRAND 241 241 FT TURN 243 244 FT STRAND 249 249 FT HELIX 252 262 FT STRAND 264 264 FT TURN 266 269 FT STRAND 271 271 FT STRAND 274 276 FT TURN 277 278 FT STRAND 281 281 FT HELIX 284 286 FT STRAND 287 287 FT STRAND 289 290 FT TURN 291 292 FT STRAND 293 293 FT STRAND 297 299 FT STRAND 303 304 FT STRAND 307 309 FT TURN 311 312 FT STRAND 315 315 FT STRAND 318 320 FT STRAND 322 322 FT TURN 323 324 FT STRAND 326 328 FT TURN 330 331 FT STRAND 333 334 FT STRAND 336 338 FT TURN 340 341 FT STRAND 346 348 FT STRAND 350 351 FT STRAND 354 356 FT STRAND 359 360 FT STRAND 363 365 FT STRAND 368 369 FT STRAND 372 374 FT STRAND 377 378 FT STRAND 381 383 FT STRAND 386 387 FT STRAND 390 392 FT HELIX 396 399 FT STRAND 400 400 FT TURN 401 402 FT STRAND 403 403 FT STRAND 405 409 FT TURN 412 414 FT STRAND 415 418 FT HELIX 420 426 FT TURN 427 427 FT TURN 429 430 FT STRAND 431 434 FT STRAND 436 437 FT STRAND 440 440 FT TURN 442 443 FT STRAND 444 450 FT TURN 451 454 FT STRAND 455 460 FT STRAND 462 463 FT STRAND 466 467 FT STRAND 469 476 FT TURN 480 482 FT STRAND 483 485 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 //