ID A0A101UP01_9ACTN Unreviewed; 361 AA.
AC A0A101UP01;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KUO14248.1};
GN ORFNames=AQJ58_02395 {ECO:0000313|EMBL:KUO14248.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO14248.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO14248.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO14248.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL Submitted (OCT-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 -!- 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:KUO14248.1}.
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DR EMBL; LMXA01000001; KUO14248.1; -; Genomic_DNA.
DR RefSeq; WP_067245668.1; NZ_KQ949023.1.
DR AlphaFoldDB; A0A101UP01; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000053431; 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:SF3; SLL1280 PROTEIN; 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:UP000053431};
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 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..273
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 39982 MW; 43B5BC14F629307A CRC64;
MSDDGRQNHG SENVPSRQRT RFPGISSRAY EHPADRSALV ALRKLSGFDT VFKALSGLLP
ERSLRLLFLS DSVRVSDQQF THLNDMLRDA CYILDLEKVP PMYVNQDPQP NAMCIGLDEP
IIVVTTGLVE LLDEEEMRAV IGHEVGHALS GHAVYRTILL FLTNLAIRVA WIPLGTVAIM
AIVTALREWF RKSELSADRA GLLVGQDLQA SMRGLMKLAG GNHLHEMNVD AFLKQAEEYE
ESGDLRDSVL KILNVLPRTH PFATVRAAEL KKWAESRDHQ RIMDGHYPRR DEDKSTSVSD
SFRESASHYA STIKTSKDPL MKLVTDIAGG AGGLGGRVRR GFDGFTSTPG RNEEPPAESA
P
//
