ID A0A086ARJ5_9FLAO Unreviewed; 269 AA.
AC A0A086ARJ5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KFF19309.1};
GN ORFNames=IQ37_16305 {ECO:0000313|EMBL:KFF19309.1};
OS Chryseobacterium piperi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=558152 {ECO:0000313|EMBL:KFF19309.1, ECO:0000313|Proteomes:UP000028709};
RN [1] {ECO:0000313|EMBL:KFF19309.1, ECO:0000313|Proteomes:UP000028709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTM {ECO:0000313|EMBL:KFF19309.1,
RC ECO:0000313|Proteomes:UP000028709};
RA Pipes S.E., Stropko S.J., Newman J.D.;
RT "Genome of Chryseobacterium piperi CTM.";
RL Submitted (JUL-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFF19309.1}.
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DR EMBL; JPRJ01000039; KFF19309.1; -; Genomic_DNA.
DR RefSeq; WP_034686828.1; NZ_JPRJ01000039.1.
DR AlphaFoldDB; A0A086ARJ5; -.
DR STRING; 558152.IQ37_16305; -.
DR KEGG; cpip:CJF12_15375; -.
DR eggNOG; COG4783; Bacteria.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000028709; 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:UP000028709};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001803157"
FT DOMAIN 80..252
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29013 MW; 1F6D1E686AD46E8E CRC64;
MKITYLLGVG AMALSLAACT TNPITGRSSL QLANNSEILT MSSQEYRNTL SKSKIVTGTA
DAKRVVTVGS RIKNAAERYY QSIGRSADLA NYNWEFNLIQ SNELNAWAMP GGKVAVYTGI
LPVTKDDNGL AVVLGHEVSH ALAGHGNERI SQGMVAQYGG AILGGTITNA QWASVFQRVY
PIGSQVALLK YGRNQESEAD KMGLYLMSMA GYDPRAAIPF WSRMGSASSG GNRQPQFLST
HPNPETRISD IQRDLPKALE YYKAAGGKI
//
