PRTA_PHOLL
ID PRTA_PHOLL Reviewed; 480 AA.
AC Q7N8R3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serralysin;
DE EC=3.4.24.40;
DE AltName: Full=Secreted alkaline metalloproteinase;
GN Name=prtA; OrderedLocusNames=plu0655;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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DR EMBL; BX571861; CAE12950.1; -; Genomic_DNA.
DR RefSeq; WP_011145031.1; NC_005126.1.
DR AlphaFoldDB; Q7N8R3; -.
DR SMR; Q7N8R3; -.
DR STRING; 243265.plu0655; -.
DR MEROPS; M10.063; -.
DR EnsemblBacteria; CAE12950; CAE12950; plu0655.
DR GeneID; 24167997; -.
DR KEGG; plu:plu0655; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_025059_1_1_6; -.
DR OMA; HQSWKEN; -.
DR OrthoDB; 1907192at2; -.
DR BioCyc; PLUM243265:PLU_RS03235-MON; -.
DR Proteomes; UP000002514; Chromosome.
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; 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; 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 3: Inferred from homology;
KW Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Zinc.
FT CHAIN 1..480
FT /note="Serralysin"
FT /id="PRO_0000078178"
FT REPEAT 339..356
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 357..374
FT /note="Hemolysin-type calcium-binding 2"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 294
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="2"
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 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 52862 MW; 3361029D0280B763 CRC64;
MSLKKKISYS EDVSGSEKAN ELLKWLQAYI PGKDSNIVVE HEPSKDAAKE LIRGDYRWGH
QDDDKSKAFQ LKYSFLESKP DNMPWHISEF SAFNEAQKAA AKLSIQSWAD VANINFVETT
DAKEANVTFG FFDVSLTGSY AFAYLPTPEK TQVGTWYNAK SRTFLNNDID VNGYGRQTFT
HEIGHTLGLQ HPADYNASDK VSPTYKNSAT YFEDSRAYTV MSYFGEKNTG QDFKGIYSSA
PLLNDISAIQ AVYGANNTIR ADDTVYGFNS NTDRDFYTAK DENSKLLFTA WDTGGNDTFD
FSGFTQDQRI NLNEASFSDV GGLKGNVSIA RGVTIENAIG GSGNDVLIGN DAANTLKGGA
GDDIIYGGLG ADNLWGGEGN DTFVYLSAKE SPPLERDWIH DFVSGKDKID VSLFDLGEAG
KGGVKFVREF TGEVGEAVLR YNTVDKVNDF AINLGGEFSY DDFWVKIVGE PILESDFILS
