ID   A0A1K1LZY9_9BACT        Unreviewed;       254 AA.
AC   A0A1K1LZY9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase family M48 {ECO:0000313|EMBL:SFW16431.1};
GN   ORFNames=SAMN02910409_0601 {ECO:0000313|EMBL:SFW16431.1};
OS   Prevotellaceae bacterium HUN156.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX   NCBI_TaxID=1520830 {ECO:0000313|EMBL:SFW16431.1, ECO:0000313|Proteomes:UP000182805};
RN   [1] {ECO:0000313|EMBL:SFW16431.1, ECO:0000313|Proteomes:UP000182805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUN156 {ECO:0000313|EMBL:SFW16431.1,
RC   ECO:0000313|Proteomes:UP000182805};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FPIT01000004; SFW16431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1LZY9; -.
DR   STRING; 1520830.SAMN02910409_0601; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000182805; 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; cd07332; 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.
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:UP000182805};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          67..232
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   254 AA;  28573 MW;  6CFEBFFB3FBD4B65 CRC64;
     MKKILKESLV SAVLFFSVLF LTFQVDWMKL LNLTPTIVGD KLSEWVWNLT YTGLHEVKSD
     NVRLPVDTLV NEMCKTNGID TASISVVVSR NDEVNAYATV GRHIIINTGL IERMDNEAQL
     CAVIGHEVAH LELGHIQSGI RQQAIFQVML ILLTGNGSAD GLISITSDMI SNSITRAKED
     QADEQGARYL YAMHLDPMEM ANTLESFESY GILSYLTDHS DSKERAEHIR KMHFKKTTYR
     PILSPETWKA LKEG
//