ID A0A1L3J2P6_9FLAO Unreviewed; 272 AA.
AC A0A1L3J2P6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:APG59390.1};
GN ORFNames=LPB144_02740 {ECO:0000313|EMBL:APG59390.1};
OS Christiangramia salexigens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Christiangramia.
OX NCBI_TaxID=1913577 {ECO:0000313|EMBL:APG59390.1, ECO:0000313|Proteomes:UP000182510};
RN [1] {ECO:0000313|EMBL:APG59390.1, ECO:0000313|Proteomes:UP000182510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0144 {ECO:0000313|EMBL:APG59390.1,
RC ECO:0000313|Proteomes:UP000182510};
RA Kim E., Yi H.;
RT "Gramella sp. LPB0144 isolated from marine environment.";
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; CP018153; APG59390.1; -; Genomic_DNA.
DR RefSeq; WP_072552047.1; NZ_CP018153.1.
DR AlphaFoldDB; A0A1L3J2P6; -.
DR STRING; 1913577.LPB144_02740; -.
DR KEGG; grl:LPB144_02740; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000182510; 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:UP000182510};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 90..256
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 272 AA; 29765 MW; E4CD70DAEDC5F514 CRC64;
MKLKKTFIGL SVLLLIVACK TNPFTGERNL NFVSNDQLFP ASFAQYNQFL EENKVIKGTE
ESEMIKRTGN KIVTAAERYL NANGYQGFLK DFQWEFNLVK DDAVNAFAMP GGKVVFFTGI
LPIAENETGV AVVMAHEVAH ALADHGAQRM SAAQLQQLGA VAGSVALSGK SEQTQQIFAQ
AYGLGSTVGV MLPFSRSHET EADRIGLTLM AIAGYNPEEA ADLWRRMKAN SGGQAPPEFL
STHPSNETRI QNLEKWAPEA KAEARKYGVT KF
//