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Database: UniProt
Entry: A0A0E3M7C5_CLOSL
LinkDB: A0A0E3M7C5_CLOSL
Original site: A0A0E3M7C5_CLOSL 
ID   A0A0E3M7C5_CLOSL        Unreviewed;       595 AA.
AC   A0A0E3M7C5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=CSCA_1532 {ECO:0000313|EMBL:AKA68657.1};
OS   Clostridium scatologenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1548 {ECO:0000313|EMBL:AKA68657.1, ECO:0000313|Proteomes:UP000033115};
RN   [1] {ECO:0000313|Proteomes:UP000033115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25775 {ECO:0000313|Proteomes:UP000033115};
RA   Xie J., Zhu Z., Guo T., Song T.;
RT   "Complete Genome Sequence of the Malodorant-Producing Specialist,
RT   Clostridium scatologenes ATCC 25775.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKA68657.1, ECO:0000313|Proteomes:UP000033115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25775 {ECO:0000313|EMBL:AKA68657.1,
RC   ECO:0000313|Proteomes:UP000033115};
RX   PubMed=26210291; DOI=10.1016/j.jbiotec.2015.07.013;
RA   Zhu Z., Guo T., Zheng H., Song T., Ouyang P., Xie J.;
RT   "Complete genome sequence of a malodorant-producing acetogen, Clostridium
RT   scatologenes ATCC 25775(T).";
RL   J. Biotechnol. 212:19-20(2015).
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; CP009933; AKA68657.1; -; Genomic_DNA.
DR   RefSeq; WP_029160076.1; NZ_CP009933.1.
DR   AlphaFoldDB; A0A0E3M7C5; -.
DR   STRING; 1548.CSCA_1532; -.
DR   KEGG; csq:CSCA_1532; -.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   Proteomes; UP000033115; 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          204..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   595 AA;  69011 MW;  9DF220FC956D479E CRC64;
     MAQIKKRNEI SQQDKWKVEK IYKNVESWEK DFEKLKSMTP KLSEYAGRLS KGEKLLEYFK
     LDEEISRLAG KLAIFAHMKS DEDTANPTFQ VLRDKIYAYS AEIQSMEAFF IPEILSLKEG
     TIDKFIGDIP ELNMYKFLLE EILKKKPHVL SVEQEELIAS VSDCLNAPEK VYNMLSNADM
     TFPKIKDEKG ESIELTDVNY SSFIRSKNRT VREEAFKALF NTYKKYKNTL AASLTSNIKS
     FVFISKTRKY KSSMECSLKP NDIPIEVYNN TVDTINNNLK SLHRYVSIKK KLLGLDEMHM
     YDLYVPLIDT VQEHIEYDEA VKTVKEGLKP LGKEYLDIFD EGIEDGWVDI YPNKGKRGGA
     YSTGDYDTMP YVLLNYDYKL TDVSTLAHEM GHSIHSYYSR KNQPYIYSDY SLFCAEVAST
     TNESLLMHYL IDNEKVEKRK LYLINQELEQ IRTTVFRQVM FAEFEKITHE SIESGTPLTG
     EDLCKIWRNL NKKYFGLDMV MDEEIDMEWS RIPHFYSDFY VYQYATGYAA AHSFANAILK
     NGESAVEAYK GFLKSGSSDY PINVLRKAGV DMTTPKPLED TIKRFDELLD MLETV
//
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