PRTC_DICCH
ID PRTC_DICCH Reviewed; 479 AA.
AC P16317;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serralysin C;
DE EC=3.4.24.40;
DE AltName: Full=Secreted protease C;
DE Short=ProC;
DE Flags: Precursor;
GN Name=prtC;
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B374;
RX PubMed=2211614; DOI=10.1016/s0021-9258(17)44877-0;
RA Delepelaire P., Wandersman C.;
RT "Protein secretion in Gram-negative bacteria. The extracellular
RT metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion
RT signal analogous to that of Escherichia coli alpha-hemolysin.";
RL J. Biol. Chem. 265:17118-17125(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=B374;
RX PubMed=2722818; DOI=10.1016/s0021-9258(18)81905-6;
RA Delepelaire P., Wandersman C.;
RT "Protease secretion by Erwinia chrysanthemi. Proteases B and C are
RT synthesized and secreted as zymogens without a signal peptide.";
RL J. Biol. Chem. 264:9083-9089(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 7 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The Gly-rich repeats may be important in the extracellular
CC secretion of this metalloprotease.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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DR EMBL; M59229; AAA24860.1; -; Genomic_DNA.
DR EMBL; J04736; AAA24862.1; -; Genomic_DNA.
DR EMBL; M60395; AAA63638.1; -; Genomic_DNA.
DR PIR; A38307; A38307.
DR PDB; 1GO7; X-ray; 2.10 A; P=18-479.
DR PDB; 1GO8; X-ray; 2.00 A; P=18-479.
DR PDB; 1K7G; X-ray; 2.00 A; A=1-479.
DR PDB; 1K7I; X-ray; 1.59 A; A=1-479.
DR PDB; 1K7Q; X-ray; 1.80 A; A=1-479.
DR PDB; 3HB2; X-ray; 1.75 A; P=18-479.
DR PDB; 3HBU; X-ray; 1.77 A; P=18-479.
DR PDB; 3HBV; X-ray; 1.95 A; P=18-479.
DR PDB; 3HDA; X-ray; 2.13 A; P=18-479.
DR PDBsum; 1GO7; -.
DR PDBsum; 1GO8; -.
DR PDBsum; 1K7G; -.
DR PDBsum; 1K7I; -.
DR PDBsum; 1K7Q; -.
DR PDBsum; 3HB2; -.
DR PDBsum; 3HBU; -.
DR PDBsum; 3HBV; -.
DR PDBsum; 3HDA; -.
DR AlphaFoldDB; P16317; -.
DR SMR; P16317; -.
DR MEROPS; M10.054; -.
DR EvolutionaryTrace; P16317; -.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Zinc; Zymogen.
FT PROPEP 1..17
FT /id="PRO_0000028689"
FT CHAIN 18..479
FT /note="Serralysin C"
FT /id="PRO_0000028690"
FT REPEAT 344..361
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 362..379
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 380..397
FT /note="Hemolysin-type calcium-binding 3"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3HB2"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:1K7I"
FT TURN 445..448
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:1K7I"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:1K7I"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:1K7I"
SQ SEQUENCE 479 AA; 51601 MW; 990ED8376725DF61 CRC64;
MGKNLSLRQD DAQHALSANT SSAYNSVYDF LRYHDRGDGL TVNGKTSYSI DQAAAQITRE
NVSWNGTNVF GKSANLTFKF LQSVSSIPSG DTGFVKFNAE QIEQAKLSLQ SWSDVANLTF
TEVTGNKSAN ITFGNYTRDA SGNLDYGTQA YAYYPGNYQG AGSSWYNYNQ SNIRNPGSEE
YGRQTFTHEI GHALGLAHPG EYNAGEGDPS YNDAVYAEDS YQFSIMSYWG ENETGADYNG
HYGGAPMIDD IAAIQRLYGA NMTTRTGDSV YGFNSNTDRD FYTATDSSKA LIFSVWDAGG
TDTFDFSGYS NNQRINLNEG SFSDVGGLKG NVSIAHGVTI ENAIGGSGND ILVGNSADNI
LQGGAGNDVL YGGAGADTLY GGAGRDTFVY GSGQDSTVAA YDWIADFQKG IDKIDLSAFR
NEGQLSFVQD QFTGKGQEVM LQWDAANSIT NLWLHEAGHS SVDFLVRIVG QAAQSDIIV
