ID   PQQF_PSEPH              Reviewed;         829 AA.
AC   P55174;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Coenzyme PQQ synthesis protein F;
DE            EC=3.4.24.-;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein F;
GN   Name=pqqF;
OS   Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1124983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX   PubMed=8526497; DOI=10.1128/aem.61.11.3856-3864.1995;
RA   Schnider U., Keel C., Defago G., Haas D.;
RT   "Tn5-directed cloning of pqq genes from Pseudomonas fluorescens CHA0:
RT   mutational inactivation of the genes results in overproduction of the
RT   antibiotic pyoluteorin.";
RL   Appl. Environ. Microbiol. 61:3856-3864(1995).
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}.
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; X87299; CAA60730.1; -; Genomic_DNA.
DR   PIR; S58241; S58241.
DR   AlphaFoldDB; P55174; -.
DR   SMR; P55174; -.
DR   STRING; 1124983.PFLCHA0_c56240; -.
DR   eggNOG; COG1025; Bacteria.
DR   UniPathway; UPA00539; -.
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; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR011844; PQQ_synth_PqqF.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 3.
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   Zinc.
FT   CHAIN           1..829
FT                   /note="Coenzyme PQQ synthesis protein F"
FT                   /id="PRO_0000074412"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   829 AA;  91347 MW;  35F8A4AA9F9DC1E6 CRC64;
     MSASLFWKCS CPRRITLCPH WRPCQRLRVS LRHAPHLKRC AATLRVAAGS HDVPLAWPGL
     AHFLEHLLFL GTERFPVEQG LMAYVRAQGG QLNARTCERA TEFFFELPAS AFAGGLERLC
     EMLAQPRMSL EDQHREREVL HAEFIAWSRD ATAQRQFALF DGLHAAHPLR AFHAGNRYSL
     NLPNNAFQQA LQQFHREYYQ AGQMVLSLAG PQPLEELRAL AERYGSCLPS GQHLEQTAPP
     ALMTTGNQTY QQLSGQRLDL LFALERLPAG ATAAVDFLCT WLQSAKPGGL LAELQQRQLA
     HSLKATLLYE FAGQALLHLE FDLTSVAASA PVQVRELLTE WLGFFSAQAD WAPLREEYVL
     LQQRQIEVAS ALELSRRDSR QAADGLDESG LAALKQVLKQ LQPQAVEHFS HDWRLPPANP
     FLRSTIEAPR AGLIRGQTSA HRGLRTFAQD RSRGRKESSA LSFSQALPAD PSGSALTLRW
     QLASPAPMGL HARLLRSLAT LRDDARQAGV ELIFTSCGKD WLLKLHGLPS PMPAVLLQAL
     KALGRPAESF WQEQASVNAE APLLTIRQLL KAFSEQPQPD SPAQPDPEAL QALWASARWD
     GLGLALPAAI QEALSRTLQQ MPGTADATLC RPVPAGTGQQ WQNLPGSAGE HALLLFYPVP
     SASLADEAAW RLLGQLCQTP FYQRLRVELQ LGYGVFSAVR QRNGRTGLLF GVQSPGATVT
     EILQHIAQFL EHLPEQLQAL DEPSWNDQQQ ALAQQLQPAT LPLDQAMELL WQAKLAGHSS
     DYLPQLQGCI EALTPAIVIQ AARQLREAAG GCSALANRPC PGTPWQVAE