ID Q5D1B7_XENNE Unreviewed; 478 AA.
AC Q5D1B7;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=serralysin {ECO:0000256|ARBA:ARBA00012422};
DE EC=3.4.24.40 {ECO:0000256|ARBA:ARBA00012422};
GN Name=prtA {ECO:0000313|EMBL:AAX15945.1};
OS Xenorhabdus nematophila (Achromobacter nematophilus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=628 {ECO:0000313|EMBL:AAX15945.1};
RN [1] {ECO:0000313|EMBL:AAX15945.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Breton {ECO:0000313|EMBL:AAX15945.1};
RA Montiel R., Martins T., Cabral C.M., Lucena M., Simoes N.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP37932.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bcn14 {ECO:0000313|EMBL:ADP37932.1};
RA Ferreira R.G., Montiel R., Simoes N.;
RT "Genetic divergence and positive selection in the prtA gene of the genus
RT Photorhabdus and Xenorhabdus entomopathogenic bacteria strain in Azores.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC P1'.; EC=3.4.24.40; Evidence={ECO:0000256|ARBA:ARBA00001609};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001205-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001205-2};
CC -!- SIMILARITY: Belongs to the peptidase M10B family.
CC {ECO:0000256|ARBA:ARBA00009490}.
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DR EMBL; AY920455; AAX15945.1; -; Genomic_DNA.
DR EMBL; GU293153; ADP37932.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5D1B7; -.
DR MEROPS; M10.063; -.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 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 NCBIfam; NF035945; Zn_serralysin; 1.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
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 PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001205-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:AAX15945.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AAX15945.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001205-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 54..240
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-1"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
SQ SEQUENCE 478 AA; 52542 MW; D3D092F22D87E4C6 CRC64;
MTSKKKYSNV GLSDSHSAQD VNALLTAYVP NSDPNVRVAH EVLADEAPDE LVRGHYKWAN
KYVNSSGTLE LSYHFLKSAS DPLMRIFKVS GFSAFNEEQK DAAKLSLQSW SDVANIKFTE
VSSIYKANIT FGFFDKSVNK DYAFANLPQG QKMVYTWYNA KSHTFVDNDI DVNGYIRQTF
THEIGHTLGL EHPADYDASD EIRPNYINSA EYFEDCRAYT VMSYFSEKFT GQDFKYGYSS
APLLNDISAI QELYGANMET RKGDTVYGFN SNTDRDFMTA TDANSKLIFS VWDAGGEDTF
DFSGFTQNQR INLNAGSFSD VGGLKGNVSI ARGVVIENAI GGSGDDILVG NSADNILKGG
VGDDIIYGGL GGDHLWGGEG NDIFVYLSGK ESLKNNPDWI HDFVSGEDKI DLSDFNFGGD
GDIKFVDSFS GKAGEVLFTY DEENDVTDLE ISLGGDLAGN DFLVKVIGQP LTEADFIV
//
