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Database: UniProt
Entry: A0A0F3RQX6_9LACO
LinkDB: A0A0F3RQX6_9LACO
Original site: A0A0F3RQX6_9LACO 
ID   A0A0F3RQX6_9LACO        Unreviewed;       434 AA.
AC   A0A0F3RQX6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:KJW12004.1};
GN   ORFNames=VC81_12020 {ECO:0000313|EMBL:KJW12004.1};
OS   Levilactobacillus spicheri.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW12004.1, ECO:0000313|Proteomes:UP000033491};
RN   [1] {ECO:0000313|EMBL:KJW12004.1, ECO:0000313|Proteomes:UP000033491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP38 {ECO:0000313|EMBL:KJW12004.1,
RC   ECO:0000313|Proteomes:UP000033491};
RA   Zheng J., Ganezle M.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:KJW12004.1}.
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DR   EMBL; JZCR01000024; KJW12004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F3RQX6; -.
DR   STRING; 216463.VC81_12020; -.
DR   MEROPS; M16.A20; -.
DR   PATRIC; fig|216463.3.peg.1659; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000033491; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KJW12004.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          62..150
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..350
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   434 AA;  48442 MW;  19DC1566E0DA5746 CRC64;
     MNKQTYAQLG EAVYRTTLSN GLQVILVPKA GFHKTFAIMT TDYGSIDNVF VPRGQTAAVR
     FPDGIAHFLE HKLFEKKDHD AFDLFGQFGA SSNAFTSFTQ TSYLFATTNH LHENLDILLD
     FVQDPYFTPA TVNKEKGIIG QEIQMYDDDP GWQSYFGMIG NLYPKEPLSI DIAGTVDSID
     QITADDLYAA YRTFYHPSNM SLVLTGKLDP EQTLDWIETN QARKTFTPSA PIQRVASPAT
     QPDQVIRQTT RHLSVTRPKV SLGIRGFDTV PTGRAALTYS VAVSLIFDLL FNDTSDNYLR
     LYDANVIDDS FGYDFQVQRG AHFGQLAGDT DQPELFVSEF QAILADVFTQ LKLAEPQFDL
     VKREAIGRLI GAINSPEAIA NQYSGPLFGG TMLFDELTVL EDLRFEDLLP VAHAFWDHSV
     QTVATILPEG LRND
//
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