ID   D7AP29_THEM3            Unreviewed;       418 AA.
AC   D7AP29;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ADH60945.1};
GN   OrderedLocusNames=Tmath_1230 {ECO:0000313|EMBL:ADH60945.1};
OS   Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CCUG
OS   53645 / CIP 108742 / A3).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH60945.1, ECO:0000313|Proteomes:UP000002064};
RN   [1] {ECO:0000313|EMBL:ADH60945.1, ECO:0000313|Proteomes:UP000002064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11426 / CIP 108742 / A3
RC   {ECO:0000313|Proteomes:UP000002064};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT   mathranii str. A3.";
RL   Submitted (MAY-2010) 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; CP002032; ADH60945.1; -; Genomic_DNA.
DR   RefSeq; WP_012995236.1; NC_014209.1.
DR   AlphaFoldDB; D7AP29; -.
DR   STRING; 583358.Tmath_1230; -.
DR   KEGG; tmt:Tmath_1230; -.
DR   HOGENOM; CLU_009902_3_0_9; -.
DR   Proteomes; UP000002064; 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: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;
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;  47852 MW;  EF4FA79AEE94E9ED CRC64;
     MYERKIIEGI KVVTCKIPHA YSVYIGIWIK TGSMYEHKSI NGISHFIEHM VFKGSKLRSA
     RQIAEETDSI GGQLNGFTEK ESTCFYIKVL NTHIKQGIDI LFDMVFNPAF KEEDIEKEKQ
     VIYEEILTEL DSPEDVAYNL LAKTIWKGHP LSFPVLGTFS TVKKLNKGQI VDYYNSHYNK
     DNIVISIAGN FGDDIYEILQ KYLSKIQKTN VISQLTSPIW HKNKAFYEKD FEQVNLCIGL
     PGITYDLKKV YALAIINNAF GGGMSSRLFQ KIREDKGLVY SIYSYPSTYH HAGVFSIFAS
     MNANNFRKVY DLILNEIEEV HLKGLAEEEI DKFKEQLRIN VLMDLDSISS RMSTIGKSML
     LFNKVHTVDE ILQTIDSLTY EEINELAREI INPADMSIAV VGKLNKRDKG WLENVNNT
//