ID   PQQB_XANCP              Reviewed;         299 AA.
AC   Q8P6N0;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
GN   Name=pqqB {ECO:0000255|HAMAP-Rule:MF_00653}; OrderedLocusNames=XCC2937;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: May be involved in the transport of PQQ or its precursor to
CC       the periplasm. {ECO:0000255|HAMAP-Rule:MF_00653}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00653}.
CC   -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00653}.
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DR   EMBL; AE008922; AAM42209.1; -; Genomic_DNA.
DR   RefSeq; NP_638285.1; NC_003902.1.
DR   RefSeq; WP_011038060.1; NC_003902.1.
DR   AlphaFoldDB; Q8P6N0; -.
DR   SMR; Q8P6N0; -.
DR   STRING; 340.xcc-b100_1215; -.
DR   EnsemblBacteria; AAM42209; AAM42209; XCC2937.
DR   KEGG; xcc:XCC2937; -.
DR   PATRIC; fig|190485.4.peg.3141; -.
DR   eggNOG; COG1235; Bacteria.
DR   HOGENOM; CLU_061120_0_0_6; -.
DR   OMA; FYIPGCA; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16274; PQQB-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_00653; PQQ_syn_PqqB; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR011842; PQQ_synth_PqqB.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02108; PQQ_syn_pqqB; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis; Reference proteome; Transport.
FT   CHAIN           1..299
FT                   /note="Coenzyme PQQ synthesis protein B"
FT                   /id="PRO_0000220012"
SQ   SEQUENCE   299 AA;  32566 MW;  B333EFE2E6B00B57 CRC64;
     MRIIVLGSAA GGGHPQWNCH TPASQRAWQQ ADGAQRRTQA SIAVSADGQR WVLINASPDF
     RQQILATPAL WPQHGLRHSP IESVLLTSGE IDHIAGLLSM RESQRFSLHA SSRVLDLLAQ
     NPIFDALNPQ YVDRHPFALN TPLTLCDLQL TPFSVPGKVP LFMESRSGGD LAGSNEETLG
     LTIDDGRHRV HYIPGCAAMT DDLRARLHGA ELVFFDGTLW RDDEMVQLGV SQKTGQRMGH
     MSIDGTDGTL AAFAQLQVAR KVLIHINTTN PVLDAHSPEH AAVRAAGWDV AHDGLEISL