ID   PQQF_PSESM              Reviewed;         779 AA.
AC   Q88A79;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=PSPTO_0514;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54057.1; -; Genomic_DNA.
DR   RefSeq; NP_790362.1; NC_004578.1.
DR   AlphaFoldDB; Q88A79; -.
DR   SMR; Q88A79; -.
DR   STRING; 223283.PSPTO_0514; -.
DR   EnsemblBacteria; AAO54057; AAO54057; PSPTO_0514.
DR   KEGG; pst:PSPTO_0514; -.
DR   PATRIC; fig|223283.9.peg.528; -.
DR   eggNOG; COG1025; Bacteria.
DR   HOGENOM; CLU_021089_0_0_6; -.
DR   OMA; FHAGNRY; -.
DR   OrthoDB; 1188251at2; -.
DR   PhylomeDB; Q88A79; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000002515; 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; 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..779
FT                   /note="Coenzyme PQQ synthesis protein F"
FT                   /id="PRO_0000074414"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   779 AA;  86189 MW;  3E7A846875E0537B CRC64;
     MDALMPAPQS ADLRRITLAN GLSVALCHDS RLKRSAASLR VAAGSHDAPL AWPGLAHFLE
     HLFFLGTERF QAGENLMTFV QRHGGQVNAS TRERTTDFFF ELPQTAFAQG LERLCDMLAR
     PRMTVADQLR EREVLHAEFI AWRGDANARD QLRLLAAVNP QHPLRGFHAG NRYSLSVPNP
     AFQQALQNFY QRFYQAAQMT LCLSGPQSLA ELETLANTHG ALFASGTKVR QHAPAPLMKH
     PTSLEHIDEQ KHLLFACEHL PAKADEAVAF LCHWLNAAQP GGLIATLIER GLIESLNATP
     LYQFDGQLLL DIELNANRPS ASTIKSLLLS WLRFFKTQWP ALIEEYQRLE QRRLQMSGAL
     TLAHHHCREL PAQLSDQGAD ALRELLEQLT SNALIGSAPV DNLDSTLAEW RLPAPNPFLE
     SIAEDSPEAA LYLRWELPSA QPTLWQMLNT RLTPLIEDAR QAGVNLTFSA YGNYWQIQLN
     GLRAPMVAVI EHALQRLRHA APGPLTHAGQ ASEPLIPVRQ LLKHLADHYL ISKQAQTTGD
     LHTVWKHSRW ISFASGFCAA SQLQLNTALN ATPGTRQTDV PTLPAIRLGK RWSSEASSSS
     ENAVLVFCPA PTASVEDEAA WRLLAHLLQA PFYQRLRVEL QLGYAVFSGI RQIAGRTGLL
     FGVQSPTCSA DQLFQHIEAF IGRLPALIRT ADLPEQIRVL SAQFDPANMP DQQQADIHWQ
     AYLAGHRAHH SQALQRALSN LDTHSLLATA NQLIDAAGGW LIVASRPASA AVPLSLPER