ID   PEPF_MYCGE              Reviewed;         607 AA.
AC   P47429;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Oligoendopeptidase F homolog;
DE            EC=3.4.24.-;
GN   Name=pepF; OrderedLocusNames=MG183;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-111.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71402.1; -; Genomic_DNA.
DR   EMBL; U02198; AAD12484.1; -; Genomic_DNA.
DR   PIR; C64220; C64220.
DR   RefSeq; WP_009885868.1; NZ_AAGX01000007.1.
DR   AlphaFoldDB; P47429; -.
DR   SMR; P47429; -.
DR   STRING; 243273.MG_183; -.
DR   EnsemblBacteria; AAC71402; AAC71402; MG_183.
DR   KEGG; mge:MG_183; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_14; -.
DR   OMA; YRQTMFA; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; MGEN243273:G1GJ2-207-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..607
FT                   /note="Oligoendopeptidase F homolog"
FT                   /id="PRO_0000078167"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         391
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   607 AA;  70889 MW;  471DFFF7E3AE4ED7 CRC64;
     MKNSYKWDLS VLLNNQSLQA NFLKIQTVSE ALIKAYNNGL CFTNKTSFEQ FLAIDDKFTE
     LENRYTNYLY NKQNENNLDK EVNDAIFAYQ SFKNNHNLAF STLQQELYNH EKLIKDYLTD
     PKLAVYKRNL MLVFRDKPHQ LSSQTQSLLS QINPCFNQAE RIFNILSTAD LNLQPVVYQN
     KKYPINSVSD YQSLLENTNR GIRKACYEKW IEIYWTNRNS LSLSLVENYI QLENFAKLKN
     HPSYIAQTAF NDEIEVGFID FVYQQVAQFA KTFQAFIRLK KQIYKHVLKV NKVEPYDLTL
     TLFKTKKSYT IEQAKQDALK VLDLLGDNYI KIVKKAFNEN WIDWLADKNK YTGAYSISNV
     KGLEHFFILM NFDKTKSSLN TLVHELGHSV HSWYASQHQS QNIDPTIFYA EIASIANELL
     LCYYELQLYK NNHKQLIASL LSQINHFFGA TTRQIMFSQF EKDTLYLIRV NQKPDFKTLI
     KIYANTAVKY QGFKPEVVAN KLKKTQYQKS LSHIIAIPHF YAGNFYVYKY AIGQVAGILV
     AKKINSGDKK MKDNYFKFLS SGSSLAPLET IKLLGIDLTS PQPWQEAHNE VKRWLKIVKQ
     SFKKLQK