ID F3FJ86_PSESX Unreviewed; 649 AA.
AC F3FJ86;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Coenzyme PQQ synthesis protein F {ECO:0000256|ARBA:ARBA00015088};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein F {ECO:0000256|ARBA:ARBA00030977};
DE Flags: Fragment;
GN ORFNames=PSYJA_15357 {ECO:0000313|EMBL:EGH30272.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH30272.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH30272.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH30272.1}.
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DR EMBL; AEAH01000717; EGH30272.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FJ86; -.
DR HOGENOM; CLU_021089_0_0_6; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000004471; 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; 2.
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..134
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..331
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT NON_TER 649
FT /evidence="ECO:0000313|EMBL:EGH30272.1"
SQ SEQUENCE 649 AA; 71916 MW; EE578098C2E8DF61 CRC64;
MPAAHAADTQ RLTLANGLNV VLCHEPRLKR CAASLRVAAG SHDAPRAWPG LAHFLEHLFF
LGTERFPAGD NLMTFVQLHG GQVNASTRER TTDFFFELPQ AAFAQGLERL CDMLAKPRMD
IADQLREREV LHAEFIAWLG DSASRDQARL LTAINPQHPL RGFHAGNRYS LPVPNPAFQK
ALKDFYRGFY QAGQMTLCLT GPLPMAELQA LATNHGAVFA SGMKLKQRPP PALMASTRQA
GERNHLLFAV EDLPDKADEA VAFFCHWLNA AQPGGLVAEL IRRGLCTSLH AAPLYQFGGQ
LLLDIEFTGD PANATAISSL LFSWLGFFKA HWPTRIEEYQ RLEQRRLQMC GALALANHYC
RETPAQWSEQ RQKALSALLS KLTADVDNLD PEPLTWHLPA PNPFLDTAAD DPAEAALYLR
WQLPSPQPAF WRMLDAALKP LAEDARQAGV TLTFTAYGPY WQLQLNGLRE PMVAVLQQSL
QRLQHPDAHT LEHDEPVLIP IRQLLKQLAD HYLRSDPEVA ISDLPDVWAA SRWISLTSGF
DPARQSMLDA VLNAAPGVRQ TSPPDLPTIR AGKHWATQAS SSSEDAVLVF CPAPTTSIED
EAAWRLLAHL AQAPFYQRLR GELQLGYAVF SGLRQIDGRT GLLFGVQSP
//
