ID   A0A372EY36_9RHOB        Unreviewed;       235 AA.
AC   A0A372EY36;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:RFP90101.1};
GN   ORFNames=DZK27_02980 {ECO:0000313|EMBL:RFP90101.1};
OS   Rhodobacteraceae bacterium 63075.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2301226 {ECO:0000313|EMBL:RFP90101.1, ECO:0000313|Proteomes:UP000264392};
RN   [1] {ECO:0000313|Proteomes:UP000264392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63075 {ECO:0000313|Proteomes:UP000264392};
RA   Han S.;
RT   "Wenzhouxiangella salilacus sp. nov., a novel bacterium isolated from a
RT   saline lake in Xinjiang Province, China.";
RL   Submitted (AUG-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:RFP90101.1}.
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DR   EMBL; QVMW01000002; RFP90101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372EY36; -.
DR   OrthoDB; 7338723at2; -.
DR   Proteomes; UP000264392; 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.
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:UP000264392};
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..235
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016663949"
FT   DOMAIN          70..230
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   235 AA;  25790 MW;  2880D7995AF10BD4 CRC64;
     MSFIRKGFLA VCLLVIAGCA PMEVPQAPEG AAQPPAQLSE RRAAQQFVDV VETVEPVVER
     ECRRRTPRLN CDFRIVIDDR PNQPVNAYQT LDRNGRPIIA FTLAMIGDVR NEDELAFVMS
     HEAAHHVAGH IERQRQNAAT GALVFAGLAA LTGADAQTLE NAYEVGAVVG ARTYSKDFEL
     EADRLGTIIA ARAGYNPLRG ALFFERIPDP GDRFLGTHPP NAQRLEVVRS TMRAM
//