ID   U5RZS3_9CLOT            Unreviewed;       595 AA.
AC   U5RZS3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:AGY78240.1};
GN   ORFNames=CAETHG_4039 {ECO:0000313|EMBL:AGY78240.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY78240.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY78240.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY78240.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT   systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY78240.1; -; Genomic_DNA.
DR   RefSeq; WP_013238559.1; NZ_CP012395.1.
DR   AlphaFoldDB; U5RZS3; -.
DR   KEGG; cah:CAETHG_4039; -.
DR   PATRIC; fig|1341692.11.peg.4066; -.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   Proteomes; UP000017590; 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          205..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   595 AA;  69480 MW;  2E5DE4095A08B356 CRC64;
     MVQTKRRDEI LKEDKWKVEK IYKDIESWKK DFEKLKSMAP KLSEYAGKLF EGKKLLEYFK
     LDEEVSRLAG KLAIFAHMKN DEDTANPTFQ VLRDKIYAYS AEIKSMEAFF IPEILSLPEG
     TIDKFMKAVP ELNMYKFLLE RILKKKPHIL SVEQEELIAS VSDCLNAPEK VYSMLSNADM
     TFPKIKDERG KRVELTDVNY SGFIRSKKRS VRKEAFKSLF NTYKKYKNTL AASLTSNIKN
     FIFISKTRKY KSSMECSLKP NDISLDVYNN TIDTVNNNLK SLHRYVSIKK KLLGLHEMHM
     YDLYVPLIDT VEEHIEFDEA VKIVKEGLKP LGKEYLDIFD EGIKNGWVDI YPNKGKRGGA
     YSTGDYDTMP YVLLNYNYKL TDVSTLAHEM GHSIHSYYSR KDQPYIYSDY SLFCAEVAST
     TNESLLIHYL IDNETDKKRK LYLINQELEQ IRTTVFRQVM FAEFEKVTHE KIENETPLTG
     EDLCKIWREL NVKYFGENMV VDEEIDMEWS RIPHFYWDFY VYQYATGYAA AHSFANAILE
     NGEKAVESYK EFLKSGSSDY PINVLKKAGV DMTSPKPLED TIKRFDELLD MLETV
//