ID A0A2N9JKF7_9ACTN Unreviewed; 318 AA.
AC A0A2N9JKF7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Peptidase, M48 family {ECO:0000313|EMBL:SPD88038.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:SPD88038.1};
GN ORFNames=MPLG2_3008 {ECO:0000313|EMBL:SPD88038.1};
OS Micropruina glycogenica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Micropruina.
OX NCBI_TaxID=75385 {ECO:0000313|EMBL:SPD88038.1, ECO:0000313|Proteomes:UP000238164};
RN [1] {ECO:0000313|EMBL:SPD88038.1, ECO:0000313|Proteomes:UP000238164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:SPD88038.1};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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DR EMBL; LT985188; SPD88038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N9JKF7; -.
DR KEGG; mgg:MPLG2_3008; -.
DR Proteomes; UP000238164; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000238164};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 64..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 129..304
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 35145 MW; 390CF4328BECC834 CRC64;
MTQPPPSSQP SMQWGPPSAF TPQPGYPPSH QMPGGWAGDV PPQRLAVPTG PSVAQLRHWA
EMPFVIGGLA VTIVAGVLAI AMISYGATEL PTWALAGLLA VLTPLIAFFM IRYQFYSVAS
NGIPVTPHQL PELYAIYTEL LAKMDVPWTP NLYVINGNGV LNAFASKCQL RRAYVTLFSD
LVDVAYELND FTAVKFVLAH ELGHVKCRHV SLWRMLTTAV VRFVGLDATI IRAQEYTADR
CASYYVPEGA RTLVLLYAGK RVYRNVNIEA YMASIAAHKD GLWLKLVNLF SSHPVGFRRM
AALYQVQLRG WDVHGKML
//
