ID A0A2T0SBN3_9ACTN Unreviewed; 286 AA.
AC A0A2T0SBN3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:PRY30839.1};
GN ORFNames=CLV70_104391 {ECO:0000313|EMBL:PRY30839.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY30839.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY30839.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY30839.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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 -!- 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:PRY30839.1}.
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DR EMBL; PVZG01000004; PRY30839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0SBN3; -.
DR Proteomes; UP000239209; Unassembled WGS sequence.
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:SF2; PROTEASE HTPX HOMOLOG; 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:UP000239209};
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 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 55..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..174
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 286 AA; 31966 MW; 9B4D77BB2CFAB96D CRC64;
MSTPARHPAT SQLRHPAELP FFIIMVMLNV LIIGFIVQAA VMLPVLPERL QDTGWATAVR
SALLGLLLLV PALIVVRETQ RASVRGTAVE LSPRQYPELY RTADDFAHRL GLRRRPQIYL
SNGNGTLNAF AAQATGHDYV VLSNELFVNL YHGNQEGLRF ILGHELGHIR LHHVSLWYQL
AVAYSEPIPL LGPALSRLRE YSCDRHGAHL APEGMTGLVL LASGRHTEHV VDVDELVRQG
RSLRGFWVGL SQLPRSHPFT VRRLERLYRL GFFRAGPRPA GAEPRA
//
