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Database: UniProt
Entry: A0A1U7NJ00_9FIRM
LinkDB: A0A1U7NJ00_9FIRM
Original site: A0A1U7NJ00_9FIRM 
ID   A0A1U7NJ00_9FIRM        Unreviewed;       360 AA.
AC   A0A1U7NJ00;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=RIP metalloprotease RseP {ECO:0000313|EMBL:OLU42917.1};
GN   ORFNames=BO222_00945 {ECO:0000313|EMBL:OLU42917.1};
OS   Ileibacterium valens.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Ileibacterium.
OX   NCBI_TaxID=1862668 {ECO:0000313|EMBL:OLU42917.1, ECO:0000313|Proteomes:UP000186341};
RN   [1] {ECO:0000313|EMBL:OLU42917.1, ECO:0000313|Proteomes:UP000186341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NYU-BL-A3 {ECO:0000313|EMBL:OLU42917.1,
RC   ECO:0000313|Proteomes:UP000186341};
RA   Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA   Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT   "Description of two novel members of the family Erysipelotrichaceae:
RT   Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT   gen. nov., sp. nov.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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:OLU42917.1}.
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DR   EMBL; MPJW01000033; OLU42917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7NJ00; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000186341; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:OLU42917.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OLU42917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186341};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..345
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   360 AA;  39588 MW;  DF3E581C4ABD1604 CRC64;
     MNVIITILAF LLMLNVIVII HEAGHFFAAR SFGVHCHEFS IGMGPAIYQK QGKNTLFSIR
     ALPIGGYVMM AGEEDGSQSE DSEDDWLAKV PESERLNFKP KWQQVIIMAA GVFMNFVLAF
     LIFIGLMAAR GYVVEPAIPV IDSLTEGYPA KEAGLMPGDQ IVKIVAEDGT VCIPETTDEL
     SEFLAFNPGE STFTIERDGE NFDVKMTPHK DDETQMVLLG FTSTSPVRQI SFLEAIPEGI
     KYGLDAGGMV FRTFGQLFQG KGFESLSGPV GIYKMTDTVV SQGLLPYISL FAILSLNIGI
     FNLLPIPALD GGRILIIALE SIFRRKIPTK IVEGVIIASF VLIFGLMIFS TYNDIVRLFF
//
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