ID   D3T8F9_THEIA            Unreviewed;       596 AA.
AC   D3T8F9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=Thit_0970 {ECO:0000313|EMBL:ADD02241.1};
OS   Thermoanaerobacter italicus (strain DSM 9252 / Ab9).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=580331 {ECO:0000313|EMBL:ADD02241.1, ECO:0000313|Proteomes:UP000001552};
RN   [1] {ECO:0000313|EMBL:ADD02241.1, ECO:0000313|Proteomes:UP000001552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9252 / JCM 16815 / Ab9 {ECO:0000313|Proteomes:UP000001552};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter italicus Ab9.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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DR   EMBL; CP001936; ADD02241.1; -; Genomic_DNA.
DR   RefSeq; WP_012995044.1; NC_013921.1.
DR   AlphaFoldDB; D3T8F9; -.
DR   MEROPS; M03.007; -.
DR   KEGG; tit:Thit_0970; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000001552; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          113..182
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          203..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  69835 MW;  007FE627152C3028 CRC64;
     MEILKDRSEI EDKYKWRLED IYENENLWEE DYSKTKELLE EVLKFKGKIN TSRDLLEVLK
     LNDQIGMTAS KIFAYARMRR DEDNTNPKYQ ALTDKAMRLN IEVMSATSFI APEILSIDTQ
     KLMEMIEELE ELKIYKQYLE DLIRFKPHVL SPEEEKILAE AKTLAESVSN IYTMLNNADM
     RFPTIKDEEG KEVELTHGNF IGFMQSKDRN VRKAAFNAMY DTYKKFINTF ASTMAGNVKK
     DIFYAKTRKY NSSLEASLFE DNVGVEVYNN LIETVHSRLD VLHRYVRLKK KLLGLDELHM
     YDLYVPLIQE YDKKFTYEEA IELVLEGLKP LGDEYINLLK QGFNSRWVDV YENRGKTSGA
     YSWGTYGTHP YVLLNYHGKL SDVFTIAHEM GHSLHTYYSN ATQPYVYAGY KIFVAEVAST
     CNEAILMDYL LKNSKDEKEK LYLLNHFFEE FRGTVYRQVM FAEFEKLIHE MAERGESLTA
     EVLNKKYYEL NKLYYGDDIV VDEGISYEWA RIPHFYRNFY VYKYATGFSA AIAISQMILN
     EGKKAVERYK EFLKSGSSDY PLNLLKRAGV DLTTPKPVNE ALDVFEKLLD EFEKLM
//