ID   PQQF_PSEAE              Reviewed;         775 AA.
AC   Q9I2D2;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=PA1973;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG05361.1; -; Genomic_DNA.
DR   PIR; E83400; E83400.
DR   RefSeq; NP_250663.1; NC_002516.2.
DR   RefSeq; WP_010895593.1; NZ_QZGE01000030.1.
DR   AlphaFoldDB; Q9I2D2; -.
DR   SMR; Q9I2D2; -.
DR   STRING; 287.DR97_5875; -.
DR   PaxDb; Q9I2D2; -.
DR   PRIDE; Q9I2D2; -.
DR   EnsemblBacteria; AAG05361; AAG05361; PA1973.
DR   GeneID; 878011; -.
DR   KEGG; pae:PA1973; -.
DR   PATRIC; fig|208964.12.peg.2056; -.
DR   PseudoCAP; PA1973; -.
DR   HOGENOM; CLU_021089_0_0_6; -.
DR   InParanoid; Q9I2D2; -.
DR   OMA; FHAGNRY; -.
DR   PhylomeDB; Q9I2D2; -.
DR   BioCyc; PAER208964:G1FZ6-2011-MON; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; ISS:PseudoCAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; ISS:PseudoCAP.
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; 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..775
FT                   /note="Coenzyme PQQ synthesis protein F"
FT                   /id="PRO_0000074411"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   775 AA;  84432 MW;  5C0AB3B6DA3EA36B CRC64;
     MDHHAQHHPR SHACVLPNGL RLHLAHDPAA SRAAAWLRVA AGSHDEPSAH PGLAHFLEHL
     SFLGGAAFPG DERLMPWLQV RGGQVNASTL GKTTDYFFEV TAEHLGAGLA RLIDMLARPL
     LDIDAQRRER EVLEAEYLAR SADEQTLIDA ALALGLPAGH PLRRFAAGRR DSLALESDAF
     QRALREFHAA HYHAGNCQLW LQGPQTLDEL ERLAQRACAD LPGRAPGASP PPPPLLPFAC
     EALALRLPGP PRLVLGFALD ALRGADEQTL LAFAELLGDR SPGGLLAALG EQGLGESVAL
     RVVHRDARQA LLALTFELFD GSAAAALEAA FFDWLGALRD DAASLLAARR PLLAEPTAPL
     ERLRQRVLGL PAEIRPACLD ALRADRCLRL HLDSELDGAE ARWSAGFRLS VAPVAAAPPL
     AAQRHAWRFE LPLPPSAAAE GALFLRWRFP GVPARSRFLA LRQALRPLCG QARLGGVEMG
     LEALGEDWSL SLLGPRDRLE AAVRPALARL LAAPPDWRAN GERLSSAERR RSATGLPIRQ
     LLDALPGLLG EPLAEVDDWR RTRWDALVMQ AAMPDPRWMP GQAAGERLEP LPPRPGRHRR
     ELAVDGESAL LLFCPLPTQE VPMEAAWRLL ARLHEPAFQR RLRDELQLGY ALFCGFREVG
     ARRGLLFAAQ SPRACPARLL EHMETFLQRS AEALAQLPAR RLAGLRKALA DDLRRAPGSF
     AERARRAWAE HLGGGAGRSR LLAEAALGLS GDDLLAAQAR LLEARGGWWV LSSRR