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
//