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Database: UniProt
Entry: A0A1Z1W5I2_9ACTN
LinkDB: A0A1Z1W5I2_9ACTN
Original site: A0A1Z1W5I2_9ACTN 
ID   A0A1Z1W5I2_9ACTN        Unreviewed;       310 AA.
AC   A0A1Z1W5I2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Membrane protein {ECO:0000313|EMBL:ARX81652.1};
GN   ORFNames=SMD44_01050 {ECO:0000313|EMBL:ARX81652.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX81652.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX81652.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX81652.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP021748; ARX81652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z1W5I2; -.
DR   STRING; 67267.GCA_000716675_01085; -.
DR   KEGG; salf:SMD44_01050; -.
DR   eggNOG; COG0501; Bacteria.
DR   OrthoDB; 9785340at2; -.
DR   Proteomes; UP000195880; Chromosome.
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:UP000195880};
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..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..194
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   310 AA;  33405 MW;  1B06AD3C881F6CC0 CRC64;
     MMVPVALLLL GALTAVVAPR LLARADWVER EPVVALWVWQ CVVAGVLLCC ALSMTFSAAS
     AWQAVRGHLF APAPRGVVEA YALGPTPWAA VTAVVLACGG VWTAAMLTRE IARARTRRAK
     RRAELVVRAP LLPGEEPGAD RLVVLEGERP DAWWLPGTAP QLVITTAALR RLKGRQLDAV
     LAHEQGHAQA RHDWLLHCSG ALAAGFPQVP VFAAFRDEMH RLVELAADDV ASRRFGRLTI
     ALALVELNEE RGVFGPCPTP QAHVPQRVHR LLSARPRLTA GRRLRLTAAA ALVPVVPLLV
     AFVPALRALG
//
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