ID A0A1T5A205_9SPHI Unreviewed; 273 AA.
AC A0A1T5A205;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase family M48 {ECO:0000313|EMBL:SKB29008.1};
GN ORFNames=SAMN05661099_0230 {ECO:0000313|EMBL:SKB29008.1};
OS Daejeonella lutea.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB29008.1, ECO:0000313|Proteomes:UP000189981};
RN [1] {ECO:0000313|Proteomes:UP000189981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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; FUYR01000001; SKB29008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5A205; -.
DR STRING; 572036.SAMN05661099_0230; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000189981; 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:UP000189981};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 73..256
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 273 AA; 29056 MW; B63A5E027BC4784D CRC64;
MKRLQLFGAV AISTVLLSCS QVPLTGRSQL SLVDDAVLQQ QASEAYQQFL RDPSTRIISS
GANAQKVKSV GNKLASAINR YMNANGYGDK YNYNYQFTLV DSKEINAWCM PGGKVAVYSG
ILPVTQTDAG LATVMGHEIA HAIAQHAAER YSQMTLAQGG GAIVGAAVGG RSEGTQQIVG
QLYGLGGQLA LLKYSRNQES EADRLGLIFM AMAGYNPDEA VSFWQRMASA KEGGGAPPEF
LSSHPSDATR IAAIQALLPE ARQFYKGGRT AAN
//