ID   A0A1G9L264_9FIRM        Unreviewed;       206 AA.
AC   A0A1G9L264;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Zn-dependent protease (Includes SpoIVFB) {ECO:0000313|EMBL:SDL56039.1};
GN   ORFNames=SAMN04488502_101200 {ECO:0000313|EMBL:SDL56039.1};
OS   Dendrosporobacter quercicolus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Dendrosporobacter.
OX   NCBI_TaxID=146817 {ECO:0000313|EMBL:SDL56039.1, ECO:0000313|Proteomes:UP000214880};
RN   [1] {ECO:0000313|EMBL:SDL56039.1, ECO:0000313|Proteomes:UP000214880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1736 {ECO:0000313|EMBL:SDL56039.1,
RC   ECO:0000313|Proteomes:UP000214880};
RA   de Groot N.N.;
RL   Submitted (OCT-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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNHB01000001; SDL56039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9L264; -.
DR   STRING; 146817.SAMN04488502_101200; -.
DR   OrthoDB; 9800627at2; -.
DR   Proteomes; UP000214880; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06158; S2P-M50_like_1; 1.
DR   InterPro; IPR008915; Peptidase_M50.
DR   InterPro; IPR044537; S2P-M50-like.
DR   PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR   PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDL56039.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214880};
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        84..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..159
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   206 AA;  22863 MW;  F89935D87EBA8262 CRC64;
     MFGFDQDMIF RIPALLIALT VHEYAHARAA VWLGDPTPRF EGRLTLNPIA HLDPLGLIML
     WLFKFGWAKP VNVNPANFKD WRKGMIMVSF AGPASNIIMA VIAAIVITLL AKLHILTGWV
     AAILQLTYTY NVILAIFNLI PIPPLDGSKI VASLLPGRIA YQYESIGRYG PFILIGLIYL
     GVIGAIMYPL QFILSVMINT IVNVIF
//