ID   A0A0Q3W2C6_9BACI        Unreviewed;       408 AA.
AC   A0A0Q3W2C6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:KQL35559.1};
GN   ORFNames=AN959_06555 {ECO:0000313|EMBL:KQL35559.1};
OS   Psychrobacillus sp. FJAT-21963.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL35559.1, ECO:0000313|Proteomes:UP000051878};
RN   [1] {ECO:0000313|EMBL:KQL35559.1, ECO:0000313|Proteomes:UP000051878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL35559.1,
RC   ECO:0000313|Proteomes:UP000051878};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-2015) 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:KQL35559.1}.
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DR   EMBL; LJIY01000002; KQL35559.1; -; Genomic_DNA.
DR   RefSeq; WP_056829318.1; NZ_LJIY01000002.1.
DR   AlphaFoldDB; A0A0Q3W2C6; -.
DR   PATRIC; fig|1712028.3.peg.2575; -.
DR   Proteomes; UP000051878; 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: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; 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   Hydrolase {ECO:0000313|EMBL:KQL35559.1};
KW   Protease {ECO:0000313|EMBL:KQL35559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051878}.
FT   DOMAIN          12..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          165..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   408 AA;  45742 MW;  7AF488FBBB517E2C CRC64;
     MINKITCENG LRIVSEHIPH VRSVAVGIWV QAGSRNELPE ENGLTHFIEH MLFKGTSSRS
     AKQIAEEFDR IGGNINAFTS KENTCYYAKV LNHHATHAVE ILADMFFNST FDSNEIDKER
     QVVLEEINMV EDTPDDIVHE YLWRAMYEDN PLGSPILGTE ETLNSFTKES ILSYMKKHYI
     PENIVVSVAG DIQEGLLEYI ESLFGHFKGV NSQVATLEIP KLKATYTENS KETEQAHICL
     AYPALSVKAD NIYSLVVLNN ILGGSMSSRL FQDIREDKGL AYSIYSYHSA YEDTGVLAIY
     GGTSSNQLTE LKNCIFDTIQ TIVKNGMTET EVTNSKEQLK GNLLLGLEST NSRMSRNGKN
     ELLFGKHRSL DEVSETIDEV TLDSVQELAK EIFAHEPAIS IIMPKKVD
//