ZAPA_PROMI
ID ZAPA_PROMI Reviewed; 491 AA.
AC Q11137;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serralysin;
DE EC=3.4.24.40;
DE AltName: Full=Extracellular metalloprotease;
DE Flags: Precursor;
GN Name=zapA;
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB2000;
RX PubMed=7592325; DOI=10.1128/jb.177.20.5790-5798.1995;
RA Wassif C., Cheek D., Belas R.;
RT "Molecular analysis of a metalloprotease from Proteus mirabilis.";
RL J. Bacteriol. 177:5790-5798(1995).
CC -!- FUNCTION: One of the virulence factors produced during swarmer cell
CC differentiation of the bacteria, which seems to be associated with
CC pathogenesis. The protease activity is limited to IgA1, IgA2, as well
CC as IgG degradation.
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 -!- ACTIVITY REGULATION: Ca(2+) increases protease activity.
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=AAA86729.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U25950; AAA86729.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004247335.1; NZ_WEKJ01000009.1.
DR AlphaFoldDB; Q11137; -.
DR SMR; Q11137; -.
DR STRING; 584.AOUC001_14810; -.
DR MEROPS; M10.057; -.
DR PRIDE; Q11137; -.
DR PATRIC; fig|584.120.peg.2878; -.
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; 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 InterPro; IPR019960; T1SS_VCA0849.
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 TIGRFAMs; TIGR03661; T1SS_VCA0849; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat;
KW Secreted; Virulence; Zinc; Zymogen.
FT PROPEP 1..16
FT /evidence="ECO:0000255"
FT /id="PRO_0000028697"
FT CHAIN 17..491
FT /note="Serralysin"
FT /id="PRO_0000028698"
FT REPEAT 342..359
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 360..377
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 378..395
FT /note="Hemolysin-type calcium-binding 3"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
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 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
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 337
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 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
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 366
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 370
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 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
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 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 54000 MW; 1E6EDEE3F6243A97 CRC64;
MGSFLLKKAV GLSNISDLLD KSGIFYNYST KVLPSFDYDT AGKHIAREDS TWNGKYVIGQ
PAEVTYSFPK WEGKFNQFGN KNPYEFNELQ KEHARKSLDA WSDIANIKFT EVAVGNVDGM
KASDVKTDIT FGNIYDPNGT FQAYATLPNT YAYGKDLSGQ AWFSDYHYAG NTTPELGNYG
RLTIIHEIGH TLGLMHPGDY NAGQNVPGYL KSDYAEDSRQ YTVMSYWDEY ETGAHFQGAY
AGAPLLHDIS AMQYLYGANT TTRTGDDVYG FNSNTGIDYY TATDSNDKLI FSVWDSGGND
TFDFSGFYQD QLIDLRAGNF SDVGGLQKNV SIAQNVTIEN AIGGFGNDII HGNDADNTLI
GGEGDDIIYG HSGNNTIYGG RGQDTLHGGT GSNTFIYKEI ADSLVTAADK IMDFKTGIDK
IDLSTLIQDT FSSKILNFVD NFTGNAGEAT LSYNEVTNAS ELAINAYGYN YNPDFKIDIV
GFVNYETDFI V
