ID   G2MUH2_9THEO            Unreviewed;       603 AA.
AC   G2MUH2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=Thewi_2677 {ECO:0000313|EMBL:AEM79999.1};
OS   Thermoanaerobacter wiegelii Rt8.B1.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM79999.1, ECO:0000313|Proteomes:UP000008276};
RN   [1] {ECO:0000313|EMBL:AEM79999.1, ECO:0000313|Proteomes:UP000008276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM79999.1,
RC   ECO:0000313|Proteomes:UP000008276};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hemme C.,
RA   Woyke T.;
RT   "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1.";
RL   Submitted (AUG-2011) 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; CP002991; AEM79999.1; -; Genomic_DNA.
DR   RefSeq; WP_014063766.1; NC_015958.1.
DR   AlphaFoldDB; G2MUH2; -.
DR   STRING; 697303.Thewi_2677; -.
DR   KEGG; twi:Thewi_2677; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_1_1_9; -.
DR   Proteomes; UP000008276; 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; cd09609; 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   InterPro; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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          115..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..585
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   603 AA;  70096 MW;  5C5B263E9D34C75E CRC64;
     MSTHLLDRKD VDERLTWDLS GIFKTEEEYE ATVKKTEELT KELEEEFKGK LTTPENINKC
     LDKLRSIAEL LTLAGSYAYL AVAVDQTNTE NLQRQMKFRN VASNIESRIS FVDSEIIQQE
     EEVINKAIEG SKENANYLKE ILRKKKHALH PEVEKALSAL SPVLEVFEDI YNMAKLADMD
     FGTFKVEDKE YPLSFSLFET KWEYEKDAKV RRAAFEAFYR KLKEYQHTIA AVYQAQVQKE
     KIIATLRGFD SVIDSLLFPQ KVERDMYERQ IDLIMENLAP HIRKFAKLLQ RIHGLDEMTF
     ADLKLEVDPD FEPEVTIEEA KRYIEEGLSV FGEDYREMIR RAFSERWIDF AENRGKATGA
     FCATPYGAHP YVLINWADKM REVFVLAHEL GHAGHFYLAH QHQNIFDSRP SLYFIEAPST
     MNELLMANYL MQKNSNDKRM KRWVLSTLIS RTYYHNFVTH LLEAAYQREV YRIIDEGGSV
     TAPTLNKIKR EVLEKFWGDA VKINEGAELT WMRQPHYYMG LYPYTYSAGL TIATQVNKRY
     LEEGQKALED WKEVLKAGGT KTPVELAKMA GVDITTEKPL LDTIQYIGSI IDEIIKLTEE
     LEK
//