ID   A0A1H3ESY2_9FLAO        Unreviewed;       276 AA.
AC   A0A1H3ESY2;
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=Peptidase family M48 {ECO:0000313|EMBL:SDX81871.1};
GN   ORFNames=SAMN05444411_11015 {ECO:0000313|EMBL:SDX81871.1};
OS   Lutibacter oricola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=762486 {ECO:0000313|EMBL:SDX81871.1, ECO:0000313|Proteomes:UP000199595};
RN   [1] {ECO:0000313|EMBL:SDX81871.1, ECO:0000313|Proteomes:UP000199595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24956 {ECO:0000313|EMBL:SDX81871.1,
RC   ECO:0000313|Proteomes:UP000199595};
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|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; FNNJ01000010; SDX81871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3ESY2; -.
DR   STRING; 762486.SAMN05444411_11015; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000199595; Unassembled WGS sequence.
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; cd07331; M48C_Oma1_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199595};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          75..253
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   276 AA;  30457 MW;  71EEAA1E9DD7CCA3 CRC64;
     MKKIIALSLL VIFMVSCSTV PITGRKRINL VSDAQILPSS FAQYSTFLKE NKISTDARKT
     NEIQSVGIRI SKAVDKFMRA NNMVSEANNY RWEFNLINDN TVNAWCMPGG KVVFYTGILP
     ICANTDGIAA VMGHEVAHAF AKHGQERMTS AYAQQLGGVA VAVGTANKDP KARELWNMAY
     GVGSQLGMLA YSRTHETEAD KLGMVFMIMA GYKPEEAVNV WIRMSQRADA SKAPPEFLST
     HPSNQTRIKN LRAFLPTAMV LAKKYSTQQL PANSKQ
//