ID   A0A3M2LK88_9ACTN        Unreviewed;       313 AA.
AC   A0A3M2LK88;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=M56 family peptidase {ECO:0000313|EMBL:RMI37899.1};
GN   ORFNames=EBN88_18050 {ECO:0000313|EMBL:RMI37899.1};
OS   Streptomyces triticirhizae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2483353 {ECO:0000313|EMBL:RMI37899.1, ECO:0000313|Proteomes:UP000278673};
RN   [1] {ECO:0000313|EMBL:RMI37899.1, ECO:0000313|Proteomes:UP000278673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY642 {ECO:0000313|EMBL:RMI37899.1,
RC   ECO:0000313|Proteomes:UP000278673};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (OCT-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:RMI37899.1}.
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DR   EMBL; RFFJ01000102; RMI37899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2LK88; -.
DR   Proteomes; UP000278673; 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..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..202
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   313 AA;  33776 MW;  6AEE3819C48BC9C4 CRC64;
     MVITITLLVL GGLTAAVAPR VLARGAWADR EPVLALWMWQ CVVAAVLLCC VLAMALSGAA
     GWGTVRGGVF APAPAQVVDA YALRPAGDRW AAAVALALAC GGLWTAVALT REVRRARAQR
     RRRRAELLAR SPLLPGEAAR SAEPLVIWED ERPDAWLLPG SPPQLVITTG ALRRLNRRQL
     DAVLAHEHGH ARARHHWLQH CAGALANGFP RVPVFAAFQA QVHRLVELSA DDMASRRFGR
     LTTALALVGM NEERGVFGCH AEHGDVPRRV NRLLEPERRL TPARRLRLTA AVTLVPLVPL
     LVAFAPGLSA LTG
//