ID   Q24WB2_DESHY            Unreviewed;       601 AA.
AC   Q24WB2;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=DSY1891 {ECO:0000313|EMBL:BAE83680.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83680.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE83680.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE83680.1,
RC   ECO:0000313|Proteomes:UP000001946};
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008230; BAE83680.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24WB2; -.
DR   STRING; 138119.DSY1891; -.
DR   MEROPS; M03.007; -.
DR   KEGG; dsy:DSY1891; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   Proteomes; UP000001946; 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:UP000001946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          118..187
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          208..588
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   601 AA;  68997 MW;  ADBCDBD98DFE7C49 CRC64;
     MLMEQAKLKT RSEIPEQYKW HLEDIFPSDQ AWEEEFLKAE KLLERAESFQ GHLGDSAEAL
     LTCFDWMDEV GQSVGEIYTY ARMRRDEDNR NAHYQALTDR AGALSVRVGS ALAFVVPEIL
     ALPEGRLQEF RQANEKMALY DHALEDILRK REHVLSSQEE KLLAEMGEIA EGPSTIFGMA
     NNADLKFPSI KNEQDEEVEL TKGNYIQFME SENRRVRQEA FETLYGTYQK QINTWAAILN
     SNIKGDVFFA RARRYPSAIE ASLHDDKVPL GVYDALIDTV REFLPEMHRY VKLRKKALGL
     DELHMYDIYV PIVSEVKMTI PYQEAVAMCR EGLKPLGSDY GKVLEEGFTS HWIDVYENQG
     KTSGAYSWGT YRSHPYVLLN HQDTLDSMFT IAHEMGHSLH TYFSNRTQPH IYAGYKIFVA
     EVASTLNEAL VMDHLLKTTE DPKLLAYLLN HYLEQFRGTV FRQTMFAEFE KKTHALVEQG
     EALTAELLSS TYLKLNEDYY GPDVVMDPQI AIEWARIPHF YNAFYVYKYA TGFSAATALA
     RKILDEGEPA VERYLRFLSS GSSDYPIELL REAGVDMETP VPVREALQVF TSLLDRLEGL
     L
//