ID   A0A4Q7ZG03_9ACTN        Unreviewed;       430 AA.
AC   A0A4Q7ZG03;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:RZU49687.1};
GN   ORFNames=EV385_1440 {ECO:0000313|EMBL:RZU49687.1};
OS   Krasilnikovia cinnamomea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Krasilnikovia.
OX   NCBI_TaxID=349313 {ECO:0000313|EMBL:RZU49687.1, ECO:0000313|Proteomes:UP000292564};
RN   [1] {ECO:0000313|EMBL:RZU49687.1, ECO:0000313|Proteomes:UP000292564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45162 {ECO:0000313|EMBL:RZU49687.1,
RC   ECO:0000313|Proteomes:UP000292564};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (FEB-2019) 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:RZU49687.1}.
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DR   EMBL; SHKY01000001; RZU49687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q7ZG03; -.
DR   Proteomes; UP000292564; 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:UP000292564}.
FT   DOMAIN          19..166
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          173..351
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   430 AA;  46326 MW;  C57AF87E1BE9D80B CRC64;
     MTRTIQDGVR RTVLPSGLRV LTEHIPTAHS VSLGVWVGIG SRDEAPAMSG ASHFLEHLLF
     KGTHKRTALD ISAQIEAVGG ETNAFTTKEY TCYYARVLDA DLPLAVDVLC DAVADSVLHP
     ADVETERAVI LEEIAMHDDE PGDEVHDVFT EAIFGNHPLG RPISGTTDTI SPMTRATING
     FYRRRYTPPR IVIAAAGNLD HAAVVRLVRK ALAGTALDTP AAAPALCRPA DHRVRTQRAH
     TVVRNRDTEQ AHMVLGCPGI GRRDERRFAL GILNNVLGGG MSSRLFQEIR EKRGLAYSVY
     SYGSQYADAG VFGVYAGCAP GKAEEVLDLI RAELATVAAN GITAEEVARG KGMVKGSYVL
     GLEDTGSRMS RIAKSELLYG DLLTVSELLA RVDAVTLDEI NELAVELLSR PMSLAVVGPF
     DESAFPDTAR
//