ID   A0A367BCF0_9ACTN        Unreviewed;       312 AA.
AC   A0A367BCF0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=M56 family peptidase {ECO:0000313|EMBL:RBY97536.1};
GN   ORFNames=DQ237_00860 {ECO:0000313|EMBL:RBY97536.1};
OS   Blastococcus sp. TF02-8.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY97536.1, ECO:0000313|Proteomes:UP000252403};
RN   [1] {ECO:0000313|EMBL:RBY97536.1, ECO:0000313|Proteomes:UP000252403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-8 {ECO:0000313|EMBL:RBY97536.1,
RC   ECO:0000313|Proteomes:UP000252403};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF02-8.";
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:RBY97536.1}.
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DR   EMBL; QOHK01000001; RBY97536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367BCF0; -.
DR   OrthoDB; 9785340at2; -.
DR   Proteomes; UP000252403; 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:UP000252403};
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..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..260
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   312 AA;  33155 MW;  53D54A3BD96E4B3D CRC64;
     MTGLLALLTG ALALSLHGHR PLMWLADRRV DPTVLLTGWL LSTVGLVVSL LATTVVIALP
     ADDHPASGLF RLAGGCWTAI SSGSVPEWRE WIGAVSVLGT MGILVRLGWA VHQRLRHRQR
     RAPHVAQLRL LAAGSSPHEP LWVRDNRPLA LSIGGRPGLI VMSDALRQQL PPVAVNAALE
     HERAHLRGRH HALIAVVEVL AAALPFCTLL RVAPAAIRDL VELAADAEAA RRCGSSAVRE
     ALSRLTEQPA PSFGLGMAGR LTHTRLSRLA EENVRGRRTA RTAGCIAVAA SALLLPTAAA
     WLALNVVGCV VT
//