ID A0A0N0K2Q7_9SPHN Unreviewed; 339 AA.
AC A0A0N0K2Q7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=IP68_00290 {ECO:0000313|EMBL:KPF77416.1};
OS Blastomonas sp. AAP25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Blastomonas.
OX NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF77416.1, ECO:0000313|Proteomes:UP000037930};
RN [1] {ECO:0000313|EMBL:KPF77416.1, ECO:0000313|Proteomes:UP000037930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP25 {ECO:0000313|EMBL:KPF77416.1,
RC ECO:0000313|Proteomes:UP000037930};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF77416.1}.
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DR EMBL; LJHP01000001; KPF77416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0K2Q7; -.
DR PATRIC; fig|1523416.3.peg.57; -.
DR Proteomes; UP000037930; 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; cd07342; M48C_Oma1_like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
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 SUPFAM; SSF50156; PDZ domain-like; 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:UP000037930};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..339
FT /note="Peptidase M48 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005853037"
FT DOMAIN 189..235
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 339 AA; 36230 MW; DC29849BD0235DD9 CRC64;
MRHIVCCLAL GGALPSGAAP AFAEAPDSAI AAFDALRASD TRVLSVGTRL ARANAPFCRS
RENAIGMTLH HIGQYPDAAA ARASFGFARD YAVLALVADG PAAQAGIRPD DAIVALNGVA
FAPAPAALGT IDQPAAYRPI AWADAQIRSA LDTGPITLTL IRDGRTFDVA VTGTPACRSR
FELRPSGEYG ASADGDIVGI TVPMLDFMLD DDELAAILAH EMAHNLLEHR RRLNAAGVQR
GLLQQFGRNA RLTLATEIEA DRLSIWLMAN AGYDPAGAVR FWTRYGRQRG KGIFSAPTHY
RWKKRVGLFE EEMAKLTGAA RDPRGWLPPL LAEPLAPLD
//
