ID   A0A1X7INM0_9BACL        Unreviewed;       424 AA.
AC   A0A1X7INM0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SAMN06295960_0655 {ECO:0000313|EMBL:SMG16635.1};
OS   Paenibacillus aquistagni.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1852522 {ECO:0000313|EMBL:SMG16635.1, ECO:0000313|Proteomes:UP000193834};
RN   [1] {ECO:0000313|EMBL:SMG16635.1, ECO:0000313|Proteomes:UP000193834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11 {ECO:0000313|EMBL:SMG16635.1,
RC   ECO:0000313|Proteomes:UP000193834};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362031};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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DR   EMBL; FXAZ01000001; SMG16635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7INM0; -.
DR   STRING; 1852522.SAMN06295960_0655; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000193834; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00989; PDZ_metalloprotease; 1.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW   Metal-binding {ECO:0000256|RuleBase:RU362031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU362031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SMG16635.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193834};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362031};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362031};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        169..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        350..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          185..261
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   424 AA;  46682 MW;  3D41E3F9D0A95BD1 CRC64;
     MQMVQVVFLT VLVFFIIVTI HEWGHMIFAK RAGILVREFA IGFGPKVFSY VRGETRYTLR
     LLPVGGFVRM AGEDPEMVDL QPGQTIAVRA KDSQVSKLYL DQLDLRKNVI RGEIESLDLE
     KELKLALIVD GETMHFTVHP QAMMIVKGQE IQIAPLDRQF GSKTVGQRAL AIFAGPLMNF
     ILAFLLFGLY IQQVGMPVDN PTYVKVGEVT AGMPAEAASV KKGDIIDQVN GTVIGGDREK
     LIKLIEASEG KPMDWVINRD GEQLNLSITP VAVEGQKGGK VGIAPILPTR SATIGETVTY
     AGNAMVTMTK NIFEGFKQLI FGQFKLDDLG GPVRTFEVTG QFAKQGIDQL TLWTAILSLY
     LGIFNLLPIP ALDGSRLVFL GLEGLRGKPI DPNRESMVHF IGFAMLMLLM LAVTYNDILR
     LVKG
//