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Database: UniProt
Entry: M1MIR6_9CLOT
LinkDB: M1MIR6_9CLOT
Original site: M1MIR6_9CLOT 
ID   M1MIR6_9CLOT            Unreviewed;       633 AA.
AC   M1MIR6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=yjbG {ECO:0000313|EMBL:AGF56218.1};
GN   ORFNames=Cspa_c24530 {ECO:0000313|EMBL:AGF56218.1};
OS   Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF56218.1, ECO:0000313|Proteomes:UP000011728};
RN   [1] {ECO:0000313|EMBL:AGF56218.1, ECO:0000313|Proteomes:UP000011728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL   Submitted (FEB-2013) 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; CP004121; AGF56218.1; -; Genomic_DNA.
DR   RefSeq; WP_015392537.1; NZ_AOIF01000105.1.
DR   AlphaFoldDB; M1MIR6; -.
DR   STRING; 36745.CLSAP_22680; -.
DR   KEGG; csr:Cspa_c24530; -.
DR   PATRIC; fig|931276.5.peg.2458; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000011728; 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   Reference proteome {ECO:0000313|Proteomes:UP000011728};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..633
FT                   /note="Oligoendopeptidase F"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004015582"
FT   DOMAIN          140..203
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          230..610
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   633 AA;  72350 MW;  6E21B04A1532B31F CRC64;
     MKKNLQRKLV CVPLALSILL SQSAVFAAGP VTRDSVDQKY KWSIDDIYPT KDLFDADYKK
     VTETYIPKLN SFKGHLTSAQ SIKDCLNTKD EMMRIVEKLY VYASMKSNED ESNSPNSEKK
     SLTESLNSQV GVATAFIQTE ILAQSEDTIK KYMQDPLLAD YKHYIDRLLK EKAHTLSQGE
     EEILAAASDM ASSPDDIYSK LKTDMEGFLP TIKDPENKDF KITNSSYGSM LDNQNRDFRK
     KGFEELYSVY DKEKNSLAAT LNAEVKKNEF FAKERKYNSA EEAALADENI PVAVYDNLVS
     SVDKNVNSLH KYVTLRKKIL GVDKVHLYDM YVPLTKNFDV KIPYEDGKKL VLKGLAPLGQ
     DYIDVLSNAF ESRWADVYET NNKYSGAYQW GTYDTHPYVL MNYDESADSV LTTAHEFGHA
     MNAYYTNKTQ KYVNSEQPIF TAEVASTANE LMMLRYLINN AKTDDEKLYY INTLAEDIRG
     TVYTQTMYAE FEKMIHERVE KGEGISADSL SSMWKDLMVK YYGDDFQDDE LANLWWARIP
     HFYMNFYVYK YATSMAASNQ LVKNMTEGTD ASKAEGVKKY RNFLTSGSSD YPIETLKKAG
     VDVTTSESVD NLLKEFDQLV DQMDQILSKQ QKK
//
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