ID Q49GQ6_PHOLM Unreviewed; 484 AA.
AC Q49GQ6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=serralysin {ECO:0000256|ARBA:ARBA00012422};
DE EC=3.4.24.40 {ECO:0000256|ARBA:ARBA00012422};
GN Name=prtA {ECO:0000313|EMBL:AAX99103.1};
OS Photorhabdus laumondii subsp. laumondii (Photorhabdus luminescens subsp.
OS laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=141679 {ECO:0000313|EMBL:AAX99103.1};
RN [1] {ECO:0000313|EMBL:AAX99103.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Az30 {ECO:0000313|EMBL:AAX99103.1};
RA Montiel R., Plaza E., Cabral C.M., Lucena M., Simoes N.;
RT "Genetic diversity of Photorhabdus spp. isolates from the Azores,
RT Portugal.";
RL Submitted (FEB-2005) 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; AY928059; AAX99103.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49GQ6; -.
DR MEROPS; M10.063; -.
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; 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 Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF13688; Reprolysin_5; 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:ARBA00023049, ECO:0000313|EMBL:AAX99103.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001205-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:AAX99103.1}; Protease {ECO:0000313|EMBL:AAX99103.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001205-2}.
FT DOMAIN 73..243
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-1"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
SQ SEQUENCE 484 AA; 53406 MW; 8D8899E4B5565524 CRC64;
MEKYMSLKKK ISYSEDVSGS EKANELLKWL QAYIPGKDSN IVVEHEPSKD AAKELIRGDY
RWGHQDDDKS KAFQLKYSFL ESKPDNMPWH ISEFSAFNEA QKAAAKLSIQ SWADVANINF
VETTDAKEAN VTFGFFDVSL TGSYAFAYLP TPEKTQVGTW YNAKSRTFLN NDIDVNGYGR
QTFTHEIGHT LGLQHPADYN ASDKVSPTYK NSATYFEDSR AYTVMSYFGE KNTGQDFKGI
YSSAPLLNDI SAIQAVYGAN NTIRADDPVY GFNSNPDRDF YTAKDENSKL LFTAWDTGGN
DTFDFSGFTQ DQRINLNEAS FSDVGGLKGN VSIARGVTIE NAIGGSGNDV LIGNDAANTL
KGGAGDDIIY GGLGADNLWG GEGNDTFVYL SAKESPPLER DWIHDFVSGK DKIDVSLFDL
GEAGKGGVKF VREFTGEVGE AVLRYNTVDK VNDFAINLGG EFSYDDFWVK IVGEPILESD
FILS
//
