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
//