ID   PQQF_KLEPN              Reviewed;         761 AA.
AC   P27508;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15380 / DSM 2026 / NCTC 418 / NCIMB 418;
RX   PubMed=1313537; DOI=10.1007/bf00280008;
RA   Meulenberg J.J.M., Sellink E., Riegman N.H., Postma P.W.;
RT   "Nucleotide sequence and structure of the Klebsiella pneumoniae pqq
RT   operon.";
RL   Mol. Gen. Genet. 232:284-294(1992).
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.
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; X58778; CAA41584.1; -; Genomic_DNA.
DR   PIR; S20458; S20458.
DR   RefSeq; WP_004225013.1; NZ_UGLG01000003.1.
DR   AlphaFoldDB; P27508; -.
DR   SMR; P27508; -.
DR   MEROPS; M16.006; -.
DR   BioCyc; MetaCyc:MON-15351; -.
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; 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   Zinc.
FT   CHAIN           1..761
FT                   /note="Coenzyme PQQ synthesis protein F"
FT                   /id="PRO_0000074410"
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   761 AA;  83617 MW;  187182DBC8E839B5 CRC64;
     MTLATRTVTL PGGLQATLVH QPQADRAAAL ARVAAGSHHE PSRFPGLAHL LEHLLFYGGE
     RYQDDDRLMG WVQRQGGSVN ATTLARHSAF FFEVAADALA DGVARLQEML QAPLLLREDI
     QREVAVIDAE YRLIQQHEPS RREAAVRHAA SAPAAFRRFQ VGSADALAGD LAALQAALGD
     FHRTHYVARR MQLWLQGPQS LEALGELAAR FAAGLAAGEA PPPAPPLRLG EFTALQLAVS
     SQPALWRCPL IALSDNVTLL REFLLDEAPG SLMAGLRQRR LAGDVALNWL YQDRHLGWLA
     LVFASDRPEE VDRQITHWLQ ALQQTTPEQQ QHYYQLSRRR FQALSPLDQL RQRAFGFAPG
     APPAGFADFC AALQVAPSVS LACQTVSPGE PVATQGFSLP LSRWRRRPES DPALAFAFYP
     QAAGDLVAKC PEKAAPLLHL PSPGDPPRLL LRPPFYCSPD QAEGLARGEQ LRPLLAALRH
     AGGHGEWHLF DGSWQLTLQL PEPGRRPEAI LQAILRQLAL PVASLTPSPE SIAIRHLMAQ
     LPERLGTSGH QKGWLAALAG GSAEDAQWVA RQLSLITAPV NPPMPAPAPC RRGVERLVYP
     GGDTALLVFI PLPDGASLAA LRLLAQHCEP LFFQRLRVEQ QIGYVVSCRY QRVADRDGLL
     MALQSPDRRA GELLRCGKDF LRQLAPMDEA TFRPLQQRLA AQIRASRPPE ARALSALRQE
     YGLPELTPQA VDALRVAEVA DLAREMTRRR RRWQVLFTTG D