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Database: UniProt
Entry: A0A367A5U6_9ACTN
LinkDB: A0A367A5U6_9ACTN
Original site: A0A367A5U6_9ACTN 
ID   A0A367A5U6_9ACTN        Unreviewed;       311 AA.
AC   A0A367A5U6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=M56 family peptidase {ECO:0000313|EMBL:RBY84834.1};
GN   ORFNames=DQ241_16045 {ECO:0000313|EMBL:RBY84834.1};
OS   Blastococcus sp. TF02A-30.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250580 {ECO:0000313|EMBL:RBY84834.1, ECO:0000313|Proteomes:UP000253175};
RN   [1] {ECO:0000313|EMBL:RBY84834.1, ECO:0000313|Proteomes:UP000253175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02A-30 {ECO:0000313|EMBL:RBY84834.1,
RC   ECO:0000313|Proteomes:UP000253175};
RA   Ennis N., Dharumadurai D., Sevigny J., Morris K., Simpson S., Thomas W.K.,
RA   Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF02-30.";
RL   Submitted (JUL-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:RBY84834.1}.
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DR   EMBL; QOHJ01000007; RBY84834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367A5U6; -.
DR   OrthoDB; 9785340at2; -.
DR   Proteomes; UP000253175; 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   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:UP000253175};
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        36..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..199
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   311 AA;  32449 MW;  DB4DA1FF193F018F CRC64;
     MTALVALVVG ALLFGWHGHR VLMWLADRRL DPTILLTGWV LSTLGFVASL LAMLSLVALP
     VDEHHSGAFG LAGDCWMALS SGVLPGTAEA VAATGVLTAT FVVARVGLVI HARLQRRRRN
     APHMQQLRLL AAGCRAHDPL WIDDERPMAL SIGGRSGLIV MSRGLRNQLT PAAVNATLEH
     ERAHLRGRHH LILAIVETLA LALPWCPLLR AAPEAARDLV ELAADSRAAR TCGPSAVREA
     LSRLTGQPLP AGALAMAGRL TTARLQRLST GSIGGSGLSR LAGCSAVAAG ALLLPTAAAA
     LAVSAVQCAF A
//
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