ID   B0K1C8_THEPX            Unreviewed;       418 AA.
AC   B0K1C8;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Processing peptidase {ECO:0000313|EMBL:ABY92923.1};
DE            EC=3.4.24.64 {ECO:0000313|EMBL:ABY92923.1};
GN   OrderedLocusNames=Teth514_1637 {ECO:0000313|EMBL:ABY92923.1};
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY92923.1, ECO:0000313|Proteomes:UP000002155};
RN   [1] {ECO:0000313|EMBL:ABY92923.1, ECO:0000313|Proteomes:UP000002155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514 {ECO:0000313|EMBL:ABY92923.1,
RC   ECO:0000313|Proteomes:UP000002155};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) 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}.
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DR   EMBL; CP000923; ABY92923.1; -; Genomic_DNA.
DR   RefSeq; WP_009052389.1; NC_010320.1.
DR   AlphaFoldDB; B0K1C8; -.
DR   KEGG; tex:Teth514_1637; -.
DR   HOGENOM; CLU_009902_3_0_9; -.
DR   Proteomes; UP000002155; Chromosome.
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:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:ABY92923.1}.
FT   DOMAIN          12..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          165..337
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   418 AA;  47764 MW;  683E9E5F378B2A88 CRC64;
     MYEQKIIEGV KVVTCKIPHA YSVYIGIWIK AGSMYEHKTI NGISHFIEHM VFKGSKLRSA
     KQIAEETDSI GGQLNGFTEK ESTCFYIKVL NTHVKQGLDI LFDMVFNPAF KEEDIEKEKQ
     VIFEEILTEL DSPEDVAYNL LAKTIWNGHP LSFPVLGTFS TVKKLNKGQI VDYYNSHYNK
     DNIVISIAGN FGDDIYEILQ KYLSKIQKTN VISQLTSPIW HKNKAFYEKD FEQVNLCIGL
     PGITYDLRKV YALAIINNAF GGGMSSRLFQ KIREDKGLVY SIYSYPSTYH HAGVFSIFAS
     MNANNFRKVY NLILKEMEEV HSKGLAKEEI DKFKEQLRIN VLMDLDSISS RMSTIGKSML
     LFNKVYTVEE ILQTIDNLTY DEINDLAKKI INPADMSIAV VGKLNKRDKG WLENVNNT
//