PRZN_SERMA
ID PRZN_SERMA Reviewed; 487 AA.
AC P23694;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Serralysin;
DE EC=3.4.24.40;
DE AltName: Full=Extracellular metalloproteinase;
DE AltName: Full=Zinc proteinase;
DE Flags: Precursor;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SM6;
RX PubMed=2274043; DOI=10.1007/bf00633854;
RA Braunagel S.C., Benedik M.J.;
RT "The metalloprotease gene of Serratia marcescens strain SM6.";
RL Mol. Gen. Genet. 222:446-451(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=HR-3;
RX PubMed=16391997; DOI=10.1007/s00284-005-0089-8;
RA Tao K., Long Z., Liu K., Tao Y., Liu S.;
RT "Purification and properties of a novel insecticidal protein from the
RT locust pathogen Serratia marcescens HR-3.";
RL Curr. Microbiol. 52:45-49(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=8089845; DOI=10.1006/jmbi.1994.1576;
RA Baumann U.;
RT "Crystal structure of the 50 kDa metallo protease from Serratia
RT marcescens.";
RL J. Mol. Biol. 242:244-251(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX PubMed=7752231; DOI=10.1006/jmbi.1995.0249;
RA Baumann U., Bauer M., Letoffe S., Delepelaire P., Wandersman C.;
RT "Crystal structure of a complex between Serratia marcescens metallo-
RT protease and an inhibitor from Erwinia chrysanthemi.";
RL J. Mol. Biol. 248:653-661(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Baumann U.;
RL Submitted (MAR-1997) to the PDB data bank.
CC -!- FUNCTION: Has insecticidal activity against the locust M.palpalis. When
CC administered orally to locusts at a low dose it causes them to lie on
CC their sides exhibiting sporadic limb movements and muscular twitching,
CC followed by full recovery. When administered at higher doses the same
CC symptoms are observed, followed by death.
CC {ECO:0000269|PubMed:16391997}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40; Evidence={ECO:0000269|PubMed:16391997};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16391997};
CC Note=Binds 7 Ca(2+) ions per subunit. {ECO:0000269|PubMed:16391997};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16391997};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16391997};
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA39139.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X55521; CAA39137.1; -; Genomic_DNA.
DR EMBL; X55521; CAA39138.1; ALT_INIT; Genomic_DNA.
DR EMBL; X55521; CAA39139.1; ALT_INIT; Genomic_DNA.
DR PIR; S12164; S12164.
DR PDB; 1AF0; X-ray; 1.80 A; A=17-487.
DR PDB; 1SAT; X-ray; 1.75 A; A=17-487.
DR PDB; 1SMP; X-ray; 2.30 A; A=17-487.
DR PDB; 4I35; X-ray; 1.50 A; A=19-487.
DR PDB; 5D7W; X-ray; 1.10 A; A=20-487.
DR PDBsum; 1AF0; -.
DR PDBsum; 1SAT; -.
DR PDBsum; 1SMP; -.
DR PDBsum; 4I35; -.
DR PDBsum; 5D7W; -.
DR AlphaFoldDB; P23694; -.
DR SMR; P23694; -.
DR MINT; P23694; -.
DR STRING; 273526.SMDB11_4311; -.
DR MEROPS; M10.051; -.
DR EvolutionaryTrace; P23694; -.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0001907; P:killing by symbiont of host cells; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd04277; ZnMc_serralysin_like; 1.
DR Gene3D; 2.150.10.10; -; 1.
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_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR016294; Pept_M10B.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034033; Serralysin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 1.
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; SSF51120; 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; Metal-binding;
KW Metalloprotease; Protease; Repeat; Secreted; Toxin; Virulence; Zinc;
KW Zymogen.
FT PROPEP 1..16
FT /id="PRO_0000028693"
FT CHAIN 17..487
FT /note="Serralysin"
FT /id="PRO_0000028694"
FT REPEAT 348..365
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 366..383
FT /note="Hemolysin-type calcium-binding 2"
FT ACT_SITE 193
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT CONFLICT 14
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1AF0"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:5D7W"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:4I35"
FT STRAND 470..477
FT /evidence="ECO:0007829|PDB:5D7W"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:5D7W"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:5D7W"
SQ SEQUENCE 487 AA; 52105 MW; 8689FC84D83CAA2C CRC64;
MQSTKKAIEI TESSLAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ AGLFITRENQ
TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE QQQQAKLSLQ SWADVANITF
TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP
ATEDYGRQTF THEIGHALGL SHPGDYNAGE GNPTYNDVTY AEDTRQFSLM SYWSETNTGG
DNGGHYAAAP LLDDIAAIQH LYGANPSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW
DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG SGNDVIVGNA
ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS APGASDWIRD FQKGIDKIDL
SFFNKEANSS DFIHFVDHFS GTAGEALLSY NASSNVTDLS VNIGGHQAPD FLVKIVGQVD
VATDFIV
