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Database: UniProt
Entry: A0A2R7YTZ5_9ACTN
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ID   A0A2R7YTZ5_9ACTN        Unreviewed;       338 AA.
AC   A0A2R7YTZ5;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:PUA79845.1};
GN   ORFNames=C7S10_17435 {ECO:0000313|EMBL:PUA79845.1};
OS   Nocardioides currus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2133958 {ECO:0000313|EMBL:PUA79845.1, ECO:0000313|Proteomes:UP000244867};
RN   [1] {ECO:0000313|EMBL:PUA79845.1, ECO:0000313|Proteomes:UP000244867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IB-3 {ECO:0000313|EMBL:PUA79845.1,
RC   ECO:0000313|Proteomes:UP000244867};
RA   Keele B.F.;
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:PUA79845.1}.
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DR   EMBL; PYXZ01000008; PUA79845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7YTZ5; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000244867; 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};
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:UP000244867};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          68..263
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   338 AA;  37318 MW;  0B41682585F7B925 CRC64;
     MAKNVTRSRV RLTSISSRAW EHPADRGALV ALRKLKGFDT VLKTLNGLVN ERQWRLLLLG
     SAVKADERQF TRLHHLLADV GATLDATDLP ELYVRASPAF NAETIGMNKP VIVINSGMVD
     LLDDEELRFV IAHELGHALS GHAVYHTLLH RLLNVSGIFY ALPGGALGIR ALIAALREWS
     RKSELSADRA GLLATQDPAV ATRVHMKLAS GGHLDDLDIT SFFAQASEYE ETEDLRDSVL
     KMFLVENRTH PFNVVRAAEL RRWTESGDYT AILRGTYPRR EDDAEAKVSD AAQDAAKSYS
     TAFANTQDAL GRMVHDVAGF MGSAKLWIDE KFGSRGTE
//
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