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Database: UniProt
Entry: A0A0R2DJG3_9LACO
LinkDB: A0A0R2DJG3_9LACO
Original site: A0A0R2DJG3_9LACO 
ID   A0A0R2DJG3_9LACO        Unreviewed;       416 AA.
AC   A0A0R2DJG3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Protease {ECO:0000313|EMBL:KRN04185.1};
GN   ORFNames=FC86_GL000282 {ECO:0000313|EMBL:KRN04185.1};
OS   Holzapfeliella floricola DSM 23037 = JCM 16512.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Holzapfeliella.
OX   NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04185.1, ECO:0000313|Proteomes:UP000051378};
RN   [1] {ECO:0000313|EMBL:KRN04185.1, ECO:0000313|Proteomes:UP000051378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04185.1,
RC   ECO:0000313|Proteomes:UP000051378};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN04185.1}.
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DR   EMBL; AYZL01000016; KRN04185.1; -; Genomic_DNA.
DR   RefSeq; WP_056974447.1; NZ_AYZL01000016.1.
DR   AlphaFoldDB; A0A0R2DJG3; -.
DR   STRING; 1423744.FC86_GL000282; -.
DR   PATRIC; fig|1423744.4.peg.289; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000051378; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase 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; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF134; ZINC-DEPENDENT PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KRN04185.1};
KW   Protease {ECO:0000313|EMBL:KRN04185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051378}.
FT   DOMAIN          53..165
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..347
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   416 AA;  48331 MW;  BCB9433B9FA8931C CRC64;
     MITNQYHEKV YQHTFSNGFE LFYIEKRGFI QKFAGIMINY GGADQPGDFV LPAGTAHFLE
     HQLFAKPYGD ITDKFEQYEG SSNAFTSYNE TMYFASFTHQ AYENIKTLVE LVAKPYFTEK
     NVTTEREIIL QELKMYQDMP DWQLNNRLMH LMYGNESLSQ EVVGTEDALD NITAETLTTA
     YNHYYYSKNM KLIVVGDLDF NQLVSEIEED VMQINDKSNM VSEEKSSKIE LKSQMSKISG
     KVESPKFSIG IKFDEQDFSV KRPQLYIAMQ IIMENLFGLS GQFYQNLQSK GLINGEIDFD
     INFNRQGDFA VISGSSENPE ETVHKIVKQF YQASISNVEF EKQKRKLFGQ EIRQLDDFES
     YGIEFIESVF DHEDYYQYYT DIQDFSFDDC VSLISEIKNK SVHQSVILFS QNNVDK
//
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