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Database: UniProt
Entry: A0A1G5LUH8_9ACTN
LinkDB: A0A1G5LUH8_9ACTN
Original site: A0A1G5LUH8_9ACTN 
ID   A0A1G5LUH8_9ACTN        Unreviewed;       311 AA.
AC   A0A1G5LUH8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Signal transducer regulating beta-lactamase production, contains metallopeptidase domain {ECO:0000313|EMBL:SCZ15938.1};
GN   ORFNames=SAMN02745898_11555 {ECO:0000313|EMBL:SCZ15938.1};
OS   Streptomyces sp. 136MFCol5.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCZ15938.1, ECO:0000313|Proteomes:UP000199326};
RN   [1] {ECO:0000313|EMBL:SCZ15938.1, ECO:0000313|Proteomes:UP000199326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCZ15938.1,
RC   ECO:0000313|Proteomes:UP000199326};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMVI01000015; SCZ15938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5LUH8; -.
DR   OrthoDB; 9785340at2; -.
DR   Proteomes; UP000199326; 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   Reference proteome {ECO:0000313|Proteomes:UP000199326};
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        34..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..196
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   311 AA;  33442 MW;  4B124D6C4AEC968B CRC64;
     MLVSLALLLL GALAAVVTPR LMARAEWPER EPVVALWVWQ CVVAGVLLSF GLSMTFSAAA
     AWQAVRGQVF APAPHAVVEA YALAAYGPWS AVIAVLLALG GVWSGAMLTR EVRRARLRRR
     RRRAELLVRS PLMPGEEAGS GPLVVLEGER PDAWWLPGTA PQLVITTAAL GRLKGRQLDA
     VLAHEQGHAQ ARHDWLLHCS AALATGFPQV PVFAAFRDEM HRLVELAADD VASRRFGRLT
     IALALVELNE DRGVFGPCPT PDAQLPLRVN RLLSPVERLT AGRRLRLTAA AALVPVVPLL
     VAFVPGLSAL G
//
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