ID   A0A372JKA1_9ACTN        Unreviewed;       293 AA.
AC   A0A372JKA1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=M56 family peptidase {ECO:0000313|EMBL:RFU40236.1};
GN   ORFNames=DZF91_18350 {ECO:0000313|EMBL:RFU40236.1};
OS   Actinomadura logoneensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2293572 {ECO:0000313|EMBL:RFU40236.1, ECO:0000313|Proteomes:UP000261811};
RN   [1] {ECO:0000313|EMBL:RFU40236.1, ECO:0000313|Proteomes:UP000261811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-G17 {ECO:0000313|EMBL:RFU40236.1,
RC   ECO:0000313|Proteomes:UP000261811};
RA   Shi L.;
RT   "Actinomadura jelena sp. nov., a novel Actinomycete isolated from soil in
RT   Chad.";
RL   Submitted (AUG-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:RFU40236.1}.
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DR   EMBL; QURH01000299; RFU40236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372JKA1; -.
DR   OrthoDB; 3541294at2; -.
DR   Proteomes; UP000261811; 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:UP000261811};
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        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          136..179
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   293 AA;  30636 MW;  F94A441C1A08C496 CRC64;
     MNPFTFLPVA ATLPLAFALG RLRVPLHPAW TARILVTVAA TATTSAVGTV LFVAVNYGAT
     LAPGTADRLP EWMLFGDDQP VPAELGVPAL LLFACACVAI AFVLVRSARA TRRARRLARG
     VLDVDEPLAV AVPGRRDGGV LVSRGLLRLL DGPELAVVFR HEESHLRHAH HRYLLIGALT
     AAVLPPLRPL DARLRLALER WADEDTAAAT GDRALVARTI AKVALAAAPA GGPDGLPSFA
     QAQTVERVRA LLTAPPRSNS VTGPVALLSS GLTTGPLAAA ALQLDQALGL PLL
//