ID A0A2U2I7H5_9BURK Unreviewed; 289 AA.
AC A0A2U2I7H5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:PWF55619.1};
GN ORFNames=C7C56_000920 {ECO:0000313|EMBL:PWF55619.1};
OS Massilia glaciei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF55619.1, ECO:0000313|Proteomes:UP000241421};
RN [1] {ECO:0000313|EMBL:PWF55619.1, ECO:0000313|Proteomes:UP000241421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B448-2 {ECO:0000313|EMBL:PWF55619.1,
RC ECO:0000313|Proteomes:UP000241421};
RA Wang H.;
RT "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang, China.";
RL Submitted (APR-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:PWF55619.1}.
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DR EMBL; PXWF02000017; PWF55619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2I7H5; -.
DR OrthoDB; 8750998at2; -.
DR Proteomes; UP000241421; 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 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.
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:UP000241421};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..289
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015538384"
FT DOMAIN 81..263
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 289 AA; 31271 MW; 635982116BA626BC CRC64;
MMRTKLAALL GAVACAACTS TGMPITNLRD LQSIDLGSTA KQFSKVNEAT RDFTQPEEIA
LGQGIASNVL GTAPLLQDRK AQRYVGSVGR WLAMQTERQD LPWHFAVLDD KGLNAFAAPG
GYIFITKGLL LSLKNEAELA GILAHEIAHV VRKHQLNAIR KAASQSHATE FAGMMLTAKS
QNGALLSKVV AGGIDIFAKG LDKEEEYEAD RMGVVIAARA GYDVYGLPAA LQTLQAVNPD
SDAIALMFKT HPSFTSRLER LDRVLTRSFD RFDQQPTLAA RYKASVPGR
//
