ID G8UKV0_TANFA Unreviewed; 269 AA.
AC G8UKV0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:AEW22290.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:AEW22290.1};
GN OrderedLocusNames=BFO_0441 {ECO:0000313|EMBL:AEW22290.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW22290.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) 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; CP003191; AEW22290.1; -; Genomic_DNA.
DR AlphaFoldDB; G8UKV0; -.
DR STRING; 203275.BFO_0441; -.
DR KEGG; tfo:BFO_0441; -.
DR PATRIC; fig|203275.8.peg.393; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_029002_5_0_10; -.
DR Proteomes; UP000005436; 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:UP000005436};
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..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003518174"
FT DOMAIN 91..257
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 269 AA; 29693 MW; E4FEB8D63C0F5DBC CRC64;
MNINNMKKML FFCMVALLAA SCSTVPLTGR RQMLLVSDSE LLTASLTQYD QYMKTAKKST
DKDKTATVVR VGKKIAEATE TYLKQNGLEN ELKHFRWEFN LINDNQVNAF CMPGGKIVVY
EGLLRLTASD DELAVVVGHE VAHAVAKHSN ERMSQGLMTQ FGASIVNAAL SERSMAMRQL
GATVFGLGAQ LGVILPYSRK HESEADYMGL VFMTMAGYNP EVAVTFWQKM STAGNGGTPE
VLSTHPSDAT RIAAIKRYLP EMGKYKMKN
//
