ID A0A327WUY9_9GAMM Unreviewed; 280 AA.
AC A0A327WUY9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M48-like protein {ECO:0000313|EMBL:RAJ96856.1};
GN ORFNames=B0I24_10766 {ECO:0000313|EMBL:RAJ96856.1};
OS Aliidiomarina maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=531312 {ECO:0000313|EMBL:RAJ96856.1, ECO:0000313|Proteomes:UP000249203};
RN [1] {ECO:0000313|EMBL:RAJ96856.1, ECO:0000313|Proteomes:UP000249203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.15366 {ECO:0000313|EMBL:RAJ96856.1,
RC ECO:0000313|Proteomes:UP000249203};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-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}.
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:RAJ96856.1}.
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DR EMBL; QLMD01000007; RAJ96856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327WUY9; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000249203; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..280
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016389219"
FT DOMAIN 63..246
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 257..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 30577 MW; FCA7C46EE59D666F CRC64;
MKRLVKTIAM AAIALSVVSA CSTSPTGRNQ LNLLPASQLD QMGAESWNQI KGQEKILQDA
EAQAYVACIT NAIAEVVPER YHRDNWEFEI FDSETINAFA LPGGYLGVYV GMIRLAENQH
QLAAVMGHEI GHVMAEHSNE RVSQNLILTG ALVGTDLAFS NRSASQRAMI MAAVGVGAQV
GYMLPFSRRH ESEADEIGMD LMARAGFDPR QAPKLWENMQ SLGGGGGPEF LSTHPSPSSR
IRDLTNQLPD AMPLYEARSS QGNLPQCRRP AWANERPQQS
//