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Database: UniProt
Entry: A0A292Z3Z9_9PSEU
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ID   A0A292Z3Z9_9PSEU        Unreviewed;       307 AA.
AC   A0A292Z3Z9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peptidase M48, Ste24p {ECO:0000313|EMBL:GAY10926.1};
GN   ORFNames=TOK_5411 {ECO:0000313|EMBL:GAY10926.1};
OS   Pseudonocardia sp. N23.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY10926.1, ECO:0000313|Proteomes:UP000222857};
RN   [1] {ECO:0000313|EMBL:GAY10926.1, ECO:0000313|Proteomes:UP000222857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N23 {ECO:0000313|EMBL:GAY10926.1,
RC   ECO:0000313|Proteomes:UP000222857};
RA   Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT   "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT   dioxane-degrading ability.";
RL   Submitted (AUG-2017) 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:GAY10926.1}.
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DR   EMBL; BEGX01000063; GAY10926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292Z3Z9; -.
DR   OrthoDB; 3541294at2; -.
DR   Proteomes; UP000222857; 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   PANTHER; PTHR34978; POSSIBLE SENSOR-TRANSDUCER PROTEIN BLAR; 1.
DR   PANTHER; PTHR34978:SF3; SLR0241 PROTEIN; 1.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM        33..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..187
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   307 AA;  31559 MW;  F308AB5D45F8077F CRC64;
     MTAIGLVVLL FLLLGLPIAA IGAAPRCARS LSPIVATAVL TTFAVSIAAG TWTVLVLVAY
     VGTAGLVPAF HPADWSAPAI ATGLPLPVAI GAAALATVLA GRGALGLART LRSDRAAITT
     VDGLPVAGDL VVLPAPEIVA YAVPARTGRR GRIVVSAGML RTLTAPQRRA LLAHERAHLV
     HHHHRYLRAA YLAAMLNPLL GPVERAVDQA VERWADDAAV REVGDRATVA EAIGVAAVVE
     SVARGGATLA AGHSDVVDRV RDLLDRPPRR PGAGVLLLLV TVLAWIVVAL LVVHTHGLVE
     AAELSGS
//
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