ID W9TEF1_9PSED Unreviewed; 841 AA.
AC W9TEF1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Coenzyme PQQ synthesis protein F {ECO:0000256|ARBA:ARBA00015088};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein F {ECO:0000256|ARBA:ARBA00030977};
GN Name=pqqF {ECO:0000313|EMBL:EXF45736.1};
GN ORFNames=BAY1663_01795 {ECO:0000313|EMBL:EXF45736.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF45736.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF45736.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF45736.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00024932}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004886}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF45736.1}.
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DR EMBL; AZSV01000019; EXF45736.1; -; Genomic_DNA.
DR RefSeq; WP_037039274.1; NZ_AZSV01000019.1.
DR AlphaFoldDB; W9TEF1; -.
DR STRING; 1439940.BAY1663_01795; -.
DR PATRIC; fig|1439940.3.peg.1783; -.
DR eggNOG; COG1025; Bacteria.
DR OrthoDB; 9811314at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000019475; Unassembled WGS sequence.
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 Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
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 NCBIfam; TIGR02110; PQQ_syn_pqqF; 1.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019475};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 28..138
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 183..343
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 841 AA; 91750 MW; 6A449F38D789CB2F CRC64;
MSSASFEFCS PPQRLVLPDG LRLGFLPQPP GGQAAALVRV HAGSHDAPAA YPGLAHFLEH
LLFLGSAAYP PAQGLMPFVQ GCGGQLNAST RERHTDYFFQ VPAEAFAEAL KRLLDMLARP
LLDPAAQRRE REVLQAEFLA RAKDRETLCD AAIGTVLAAP HPFAGFHAGH RDTLPVESAE
FQQALLGYHQ RFYHAGQLEL LVAAPCNLER LQALLRSDEC RLPAAPEVCR PLIPLPAADA
APLYLQVEGS RTYLDLAFVL DGLPDGIAVA LDVLATWLGS QAPGSLFATL RGEGWCEAVA
LRVPYWHAGQ GVIIVELQLS EQGVPARGQI VAAVRDWLGF LTRQAPWAEL WHEYVRIRQR
SLLGKEPLAC LRYWVEPAAW QPSTDAHRVQ QALQVLGAQL RGRVPIVLSV GRAAGTGERI
VNTGAGFPLQ LATDRLPDAA PRQWHWRLPE RNRWLDIRPQ PRVAPLAAMP CWVQADAASG
EGALYVRWRF DDGQPPAGLW HVLQAALRGY IPAAAQAGVE LRFENHGHGW CLTLFGYAEA
LPVVLQDLLD VLARPPASAF DEGQRLAVEA QRPGADELLL RQLMRQLPLL LDPVPPAAGL
PLLDQAALTR AWRHARWDVL AMGLAASLSG PLQDALRAMP GIPETQALPV PAAAVAHPYV
WCGFGEPAAE TALLLFCPLP LRTAPVEAAW RQLSRLMEGA FFRRLRSELQ LGYAVFCGFR
QFGERAGMFF AVQSPSASPG EILGHIETFL AGFARELDAR PAASAAGADF ARGGDLRRRA
EQIWQARLAG RDSDYPAQVE RAMAALRPED LQHQLQALRE AKGGWCVVAN AAAPDARWLG
R
//
