ID   PEPF_MYCPU              Reviewed;         613 AA.
AC   Q98QP0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Oligoendopeptidase F homolog;
DE            EC=3.4.24.-;
GN   Name=pepF; OrderedLocusNames=MYPU_3210;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family. {ECO:0000305}.
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DR   EMBL; AL445564; CAC13494.1; -; Genomic_DNA.
DR   PIR; A99552; A99552.
DR   RefSeq; WP_010925125.1; NC_002771.1.
DR   AlphaFoldDB; Q98QP0; -.
DR   SMR; Q98QP0; -.
DR   STRING; 272635.MYPU_3210; -.
DR   EnsemblBacteria; CAC13494; CAC13494; CAC13494.
DR   KEGG; mpu:MYPU_3210; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_14; -.
DR   OMA; YQREVYR; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; MPUL272635:G1GT6-321-MON; -.
DR   Proteomes; UP000000528; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.20; -; 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   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   TIGRFAMs; TIGR00181; pepF; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..613
FT                   /note="Oligoendopeptidase F homolog"
FT                   /id="PRO_0000078169"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   613 AA;  72339 MW;  3504AA247096FAF1 CRC64;
     MSKEIKEYKK YSDVPKEYRF DLDYLLEGKT IDQLFDQFLE KSKKLIKIKD SKYQNIESYL
     ESLKLEEDFN LLNNKIINYI SNNISVNVVD SHFREISQKF EFMYYSFFNQ IGDENQRILE
     HEEKITKWLL DPRLASYKKA LDFVFKSKKH RLSKEVEDYL IKVSRGNIEL YKVYGILTNS
     ELDYGYALSS DGKRKIEINL SNRFNLLKDQ DENIRKTTYL NWNKASAKHK ETLSSLLYQH
     FSKLSADALA RGYSSTVNSF LFEDQVDEKL LKNLYDKVSS NKKVFQKYYQ NYKKFFEKKN
     SKQMEAWDIY LPLVVVDEKY SIEEAQDLVL KSLEPMGSEY ISKVKEAFSS RWVDYLPVKN
     KRSGAYSIGS THGIDKKFIL MNFDGTLNSV STLSHEMGHS MHSYFSDKTQ PQSLSSYPIF
     LAEIASIFNE LMLKDYLLEV SENLETKFHI LNESILNFVG TVHRQTLWSE YEYTLYNKID
     KGEPVGTYTK IDEIYEQISQ KYKVSDLKNH HPEDEKNVIG VNVPHFYYHF YVYKYAIGMI
     VANVFYQKYK EEGKQALEFY INKFLSAGGR DWPVEILKDA GIDLYDSKIY DLAFKNFEQT
     IDQFVEIGNK LFK