ID A0A1M4YDL7_9BACT Unreviewed; 293 AA.
AC A0A1M4YDL7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase family M48 {ECO:0000313|EMBL:SHF03850.1};
GN ORFNames=SAMN02745131_01686 {ECO:0000313|EMBL:SHF03850.1};
OS Flavisolibacter ginsengisoli DSM 18119.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1121884 {ECO:0000313|EMBL:SHF03850.1, ECO:0000313|Proteomes:UP000184048};
RN [1] {ECO:0000313|EMBL:SHF03850.1, ECO:0000313|Proteomes:UP000184048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18119 {ECO:0000313|EMBL:SHF03850.1,
RC ECO:0000313|Proteomes:UP000184048};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQUU01000005; SHF03850.1; -; Genomic_DNA.
DR RefSeq; WP_072834885.1; NZ_FQUU01000005.1.
DR AlphaFoldDB; A0A1M4YDL7; -.
DR STRING; 1121884.SAMN02745131_01686; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000184048; 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; cd07324; 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:UP000184048};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..293
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012386543"
FT DOMAIN 102..268
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 293 AA; 33240 MW; FA7996FB38156CB4 CRC64;
MIRYLVLFVA LFQLMACDNL AQDTEKPVNK RAQTYSYSCI DSGVAAKPIS RKLEKAGDLI
RNLGVSRKSI TDSVQTAYGL MFHQQMVQEG EFKMVNDAAL KTKLTKVMND LLSVREDPSH
IQYAIYALKD TMINAFTFGG RIYVTSGMLE KCKGKDDLLY AIIGHEIGHS EMGHIKSTIQ
EMELSTKVFG EQTGATVFEL KKFLTASFNQ KNELEADYYG INLTNELGYD VCTAVSFWKE
MASHENRYNE LEDFFRTHPF SSLRAECLMN HIRTNFGKDC GLDKKQLLPQ VVK
//
