ID   PQQF_PSEPK              Reviewed;         766 AA.
AC   Q88QV3;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Coenzyme PQQ synthesis protein F;
DE            EC=3.4.24.-;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein F;
GN   Name=pqqF; OrderedLocusNames=PP_0381;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ)
CC       biosynthesis. It is thought that this protein is a protease that
CC       cleaves peptides bond in a small peptide (gene pqqA), providing the
CC       glutamate and tyrosine residues which are necessary for the synthesis
CC       of PQQ (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN66012.1; -; Genomic_DNA.
DR   RefSeq; NP_742548.1; NC_002947.4.
DR   RefSeq; WP_010951730.1; NC_002947.4.
DR   AlphaFoldDB; Q88QV3; -.
DR   SMR; Q88QV3; -.
DR   STRING; 160488.PP_0381; -.
DR   EnsemblBacteria; AAN66012; AAN66012; PP_0381.
DR   KEGG; ppu:PP_0381; -.
DR   PATRIC; fig|160488.4.peg.410; -.
DR   eggNOG; COG1025; Bacteria.
DR   HOGENOM; CLU_021089_0_0_6; -.
DR   OMA; FHAGNRY; -.
DR   PhylomeDB; Q88QV3; -.
DR   BioCyc; PPUT160488:G1G01-416-MON; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR011844; PQQ_synth_PqqF.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   TIGRFAMs; TIGR02110; PQQ_syn_pqqF; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; PQQ biosynthesis; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..766
FT                   /note="Coenzyme PQQ synthesis protein F"
FT                   /id="PRO_0000074413"
FT   ACT_SITE        52
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   766 AA;  84242 MW;  0AEDF15A8C6C4206 CRC64;
     MPDAIRQLTL ANGLQLTLRH APRLKRSAAA LRVHAGSHDA PAKWPGLAHF LEHLFFLGTP
     RFPLEDGLMR YVQALGGQVN ASTRERATDF FFEVPPNALG GGLERLCQML AEPDLGIERQ
     RREREVIHAE FIAWSRNPTA QQQFALLQSV SARHPLGAFH AGNRYTLALH DAAFQQALAG
     FHQRFYQGGQ ICLSLCGPQP LDELERLARQ QAELFAAGER VPQILPPPLP AMASALTFTH
     QSLPSGAEHA LELLIAYLED SRPGTWLGAL RERGWLRRFT AERLYAFAGQ LLWHLDLKLS
     ADACPDEASA LLQGWFRFIR QADREQLNHQ FGLLQHSRAH SASALELARR DSTGQPFAKL
     DTQGLQALGA LLESLPGADH GDWQLLPVDP LLKADLPHAK AQPLPAALKI SDQLPPARQF
     AALYLRWHVP SPMRQPLQRV LEQALAPLQE RCDRASVQLQ YSSAGEYWQL HCAGLPAAVL
     RAVEQALALM LKPPASCWLP CTALPPALIP IRALLKQLPD AVRGSLPPAV PACTLTQQQL
     DSLWLHTEWH GMAAGFEDTA LKALGAALEQ CPGQGSRPSP LPTWANHRWQ HAQVPGSEHA
     LLLFCPLPAA KEAAGRLLAQ LLQGPVYQRL RVDLQLGYAV FSAFRQVEGV GGLLFGVQSP
     HTDQAQVLDH LLNLLRHGVT LDPAARQALA GQFDEPAMAN ADVAEWAWQT HLATQADRLD
     VLRRSILTTR QTDLDHLLSA LLDPGSAWLC LANAAAPDTS WQGENR