ID   A0A0J1D520_9BURK        Unreviewed;      1101 AA.
AC   A0A0J1D520;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN   ORFNames=EOS_02430 {ECO:0000313|EMBL:KLU27809.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU27809.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU27809.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU27809.1}.
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DR   EMBL; AEJF01000014; KLU27809.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1D520; -.
DR   PATRIC; fig|908627.4.peg.539; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
DR   GO; GO:0031012; C:extracellular matrix; 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   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF272; ZNMC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          878..1037
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   REGION          89..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1101 AA;  106324 MW;  C591DA146FD537D2 CRC64;
     MSLSDATDLT VLLGDATTEA GFVSTSATVS SLNGGGIVTG STGDNLNILG VDVTLNATGG
     QYSLTGNGDT ANASNSSISI ASGNQATVSG SDNTVTASAS DSITLDGSGD SATAGTGSTI
     TVNGQSDSIN ASGSSIDLAA NSQATISGTG DSVVAGQSDV IDLSNATITL TAGSQVTIEG
     SGDTIIGAAN DTITVGGSGD IINGVAGDTV DVSGAGQTVD MTGGQVDMAT NTQVNVTGSD
     DGINEAAGDS LGAYGGGNTI DTTAGALTVV GSTNGSFDLV NANGDQFGGT TANGQQTGIF
     INANSQVNEV GSNDGISESA GDAVGVYGGG NTIDTTSDAL TVLGDTNGAF DLVNGSGDQI
     GVATADGQGS GIILNGNTQA NVVGSNDGIS ESAGDAVGVY GGGNTIDTTS DALTVLGDTN
     GAFDLVNGSG DQIGVATADG QGSGIVLNGN TQANVVGSND GISESAGDAV GVYGGGNTID
     TTSDALTVLG DTNGAFDTVN GSGDQLGQAT ADGQGSGIIL NGNTQADING SNDGIGESAG
     DAVGVYGGGN TIDTTSDALT VLGDTNGAFD TVNGSGDQLG QATADGQGSG IILNGNTQAD
     INGSNDGIGE SAGDAVGVYG GGNTIDTTSD ALTVLGDTNG SFDTVNGSGD QLGQATADGQ
     GSGIVLNGNT QANVNGSNDG ISESVGDSMG AYGGGNTIDT TAGALTYVSS TDGDADTINA
     SGDTLSGTTA NGQGAGISVG TDAQADIDGS NDQTSGGDGS SVTAFGSDDS LNGQQITSGT
     TGDIADNGAF SDSSGSDDSG GSDSGGGDSG GGYYGYYGFA GNQTVVQAAL GSDIGSIAQY
     DLSIGNQAGA TAAEVALHQA QEMADATPTS GTGTSVDSNN KWAGEVVTWS LASDVGSQYD
     AEVQNAFATW AAASGITFEE VTGSSQSDIQ IAFSDLNTST TGVVGYTDYQ VSNGQISDAV
     IQLEDPSQDA LVSGADGQQT YAGTDATLSQ VLLHEIGHAL GLADNSDQDS IMYYELTSSN
     QTLDSTDVAG IQSLYGSTSS AVQSSTAGTT TSAVAGQISV DHQLGQLIAG MASFNPQAAG
     NTSLTQDDHA HHHTALAASA H
//