ID A0A1X1TGH6_9MYCO Unreviewed; 306 AA.
AC A0A1X1TGH6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase M48, Ste24p {ECO:0000313|EMBL:ORV43674.1};
GN ORFNames=AWC01_05405 {ECO:0000313|EMBL:ORV43674.1};
OS Mycolicibacterium doricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=126673 {ECO:0000313|EMBL:ORV43674.1, ECO:0000313|Proteomes:UP000193564};
RN [1] {ECO:0000313|EMBL:ORV43674.1, ECO:0000313|Proteomes:UP000193564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44339 {ECO:0000313|EMBL:ORV43674.1,
RC ECO:0000313|Proteomes:UP000193564};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) 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 -!- 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:ORV43674.1}.
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DR EMBL; LQOS01000017; ORV43674.1; -; Genomic_DNA.
DR RefSeq; WP_064872683.1; NZ_JACKUD010000053.1.
DR AlphaFoldDB; A0A1X1TGH6; -.
DR STRING; 126673.AWC01_05405; -.
DR OrthoDB; 9785340at2; -.
DR Proteomes; UP000193564; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; cd07326; M56_BlaR1_MecR1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
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|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:UP000193564};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..198
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 306 AA; 32377 MW; 5469DBA81F77CF4F CRC64;
MTTALWLLLY GGALAWLAPP VLRRMTGQGI SPHMGVAAWL ITVAATLAAW LVAVSMVIGA
TADSIRTGAV VTLCLELFGF SEHTPMAGRI GSVALIGVGT LTLGFGGLRM SRSLSRLRAR
SHEHAHAARI IGRPTGHPNV VVVDADRPAA YCVGGRLNTI IVTSAAIKTL NRSQLKAVLA
HEDAHISGRH HHILMGLRAL AVTLPRLPLF ATARHSVAEL LEMCADDTAA RRVGTRPLLA
GLIALAGHQP PVHEGLAAAG TAVVARAERL VTPTCRHVRW RHRICLAAAI IAMLATPALI
QLLCHH
//
