ID A0A2S1SJX5_9FLAO Unreviewed; 270 AA.
AC A0A2S1SJX5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:AWI26685.1};
GN ORFNames=HYN49_12685 {ECO:0000313|EMBL:AWI26685.1};
OS Flavobacterium pallidum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2172098 {ECO:0000313|EMBL:AWI26685.1, ECO:0000313|Proteomes:UP000244937};
RN [1] {ECO:0000313|EMBL:AWI26685.1, ECO:0000313|Proteomes:UP000244937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0049 {ECO:0000313|EMBL:AWI26685.1,
RC ECO:0000313|Proteomes:UP000244937};
RA Yi H., Baek C.;
RT "Genome sequencing of Flavobacterium sp. HYN0049.";
RL Submitted (MAY-2018) 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; CP029187; AWI26685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1SJX5; -.
DR KEGG; fpal:HYN49_12685; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000244937; Chromosome.
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:UP000244937};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..270
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015782176"
FT DOMAIN 92..254
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 270 AA; 28952 MW; 90E7A881797D0E61 CRC64;
MRKYVIISAF AVALGASCAT NPFTGKKTLN FVSNDQIFPT AFAQYKQFLT ENKVVSGSAA
AQQVQTVGNK IRIAAEKYLN SLGQKDYLNG YAWEYKLVEN KEVNAWCMPG GKIVVYSGIL
PVTKDEAGLA TVLGHEVSHA LANHGAQRMS VDQLQQLVGV GVVAATSGQS TQNQAIFQQA
YGLGSTLAVT LPFSRSNESE ADEIGLTLMA IAGYNPDQAV VFWQRMSANG GAAPPEFLST
HPSDATRIRN IKNLIPKAKA TAAKFGVVYK
//
