ID G4V2A5_PSEFL Unreviewed; 477 AA.
AC G4V2A5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Extracellular metalloprotease AprX {ECO:0000313|EMBL:ADD83023.1};
OS Pseudomonas fluorescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294 {ECO:0000313|EMBL:ADD83023.1};
RN [1] {ECO:0000313|EMBL:ADD83023.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bk3 {ECO:0000313|EMBL:ADD83023.1};
RA Aboelmy M.H., Gau A.E.;
RT "Characterisation of the extracellular metalloprotease (AprX) from
RT Pseudomonas fluorescens Bk3.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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; GQ862303; ADD83023.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V2A5; -.
DR MEROPS; M10.060; -.
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:ADD83023.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ADD83023.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001205-2}.
FT DOMAIN 64..235
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-1"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001205-2"
SQ SEQUENCE 477 AA; 49289 MW; 2D28EEB3F7479BE3 CRC64;
MSKVKDKAIV SAAQASTAYS QIDSFSHLYD RGGNLTVNGK PSYSVDQAAT QLLRDGAAYR
DFDGNGKIDL TYTFLTSATQ STMNKHGISG FSQFNAQQKA QAALAMQSWS DVANVTFTEK
ASGGDGHMTF GNYSGGQDGA AAFAYLPGTG AGYDGTSWYL TNNSYTPNKT PDLNNYGRQT
LTHEIGHTLG LAHPGDYNAG NGNPTYNDAT YGQDTRGYSL MSYWSESNTN QNFSKGGVEA
YASGPLIDDI AAIQKLYGAN LNTRAGDTTY GFNSNSGRDF LSATSNADKL VFSVWDGGGN
DTLDFSGFTQ NQKINLNATS FSDVGGLVGN VSIAKGVTVE NAFGGAGNDL IIGNQAANLI
KGGAGNDLIY GGGGADQLWG GAGSDTFVYG ASSDSKPGAA DKIFDFTSGS DKIDLSGITK
GAGVTFVNAF TGHAGDAVLS YASGTNLGTL AVDFSGHGVA DFLVTTVGQA AASDIVA
//
