ID   A0A495XJ36_9PSEU        Unreviewed;       468 AA.
AC   A0A495XJ36;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:RKT73145.1};
GN   ORFNames=DFJ66_6473 {ECO:0000313|EMBL:RKT73145.1};
OS   Saccharothrix variisporea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT73145.1, ECO:0000313|Proteomes:UP000272729};
RN   [1] {ECO:0000313|EMBL:RKT73145.1, ECO:0000313|Proteomes:UP000272729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT73145.1,
RC   ECO:0000313|Proteomes:UP000272729};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:RKT73145.1}.
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DR   EMBL; RBXR01000001; RKT73145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495XJ36; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000272729; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000272729}.
FT   DOMAIN          55..202
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          209..387
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  50718 MW;  6A4BD1C66F2E621A CRC64;
     MTGRVNGTAA GASSTRGRPL SGKLGHLQRP GSTRLLESSD AGVTVRRSVL PSGLRVITEQ
     IPGVRSASVG LWVQVGSRDE RPEVAGAAHY LEHLLFKGTA NRSAAAIAEE IDAVGGELNA
     FTAKEHTCYY AHVLDEDLPL ALDLVCDVVF EALCEPRDFE TERGVVLEEI AMRDDDPEDL
     LHDAFLDALL GEHALGRSVL GTERSIQDME RDALFGFYKR RYTLPRMVLA VAGNIDHNHV
     MRLARKQIGT RLERTGTPVA PRTGRARIAS SRKLVLHSDD TEQAHLMLGV RALDRHDERR
     FALNVLNAAL GGGMSSRLFQ EVRERRGLAY QVYSSVGMYA DTGTWSVYAG CQPDRLGDVA
     GVVRDVLSVV ASGGLTDAEV ARGKGQLRGG LVLGLEDTSS RMSRIGKGEL NYGDYLSVEQ
     TLARIDEVTG EDVAVLAREL LRRPVAAAVV GPYAHADDLP SQVHEVIS
//