ID PEPF_MYCPN Reviewed; 611 AA.
AC P54125;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Oligoendopeptidase F homolog;
DE EC=3.4.24.-;
GN Name=pepF; OrderedLocusNames=MPN_197; ORFNames=MP634;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS (Mycoplasmoides pneumoniae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 / Subtype 1;
RX PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT ribosomal protein genes.";
RL Nucleic Acids Res. 24:628-639(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 / Subtype 1;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U34795; AAC43684.1; -; Genomic_DNA.
DR EMBL; U00089; AAB96282.1; -; Genomic_DNA.
DR PIR; S62811; S62811.
DR RefSeq; NP_109885.1; NC_000912.1.
DR RefSeq; WP_010874554.1; NZ_OU342337.1.
DR AlphaFoldDB; P54125; -.
DR SMR; P54125; -.
DR STRING; 272634.MPN_197; -.
DR EnsemblBacteria; AAB96282; AAB96282; MPN_197.
DR KEGG; mpn:MPN_197; -.
DR PATRIC; fig|272634.6.peg.215; -.
DR HOGENOM; CLU_021290_2_0_14; -.
DR OrthoDB; 9766487at2; -.
DR BioCyc; MPNE272634:G1GJ3-315-MONOMER; -.
DR Proteomes; UP000000808; 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 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 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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..611
FT /note="Oligoendopeptidase F homolog"
FT /id="PRO_0000078168"
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 611 AA; 70959 MW; 8DB896D570BB215D CRC64;
MNNQYNWNLE VLLNGKSLAD NFTELKQLSE QEKALYDGGA CFQTKAKFTE FLQLQEKIEV
LENRYSNFLS NKHAENSLDK TINDALFQYE MFKSEHALVF VDFEKNLFKH EKVIRAYLQD
PALKQYQRDF ELVWRNKKHQ IDPASQKLLA QISPAWNQAD KIFNVLSTAD LNLQPVVYKG
KTYVINAVSD YQSLLENKDR GLREAAYKVW LEIYWPTRNT LSVSLVENYI QLETFAKLKK
HPNYIAKTAF DDEIDVAFID FVYEQVASFA PTFKAFQSLR KQIYKHVLKL DKAQPWDLSV
PLFKASGDYT IEQAQTDALK ILAPMGSEYL EVVKEAFRER WISWLPDKNK YTGAYSISNV
KGLDHYFILM NFDKTRASLN TLVHELGHSV HSWYASKYQT QNLDPTIFYA EIASICNELL
LCYHDIINYE NRNPQQLIRS LMEQISHFFG ATTRQLMFSQ FEQDTLKLIQ QNQKPDFKTL
VEIYGKTAIK YQAANADAIT KKLKQTKYQK SLAYITSIPH FYAGNFYVYK YAIGQVVGTL
VGKKLSAGDS NMLAAYKRFL SSGSTLPPLE TIKLLGIDLT QPEPWQEAHA ELKRWIKLVQ
TAFKQLQHKK R
//
