ID Q1QZA6_CHRSD Unreviewed; 299 AA.
AC Q1QZA6;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000256|ARBA:ARBA00015084, ECO:0000256|HAMAP-Rule:MF_00653};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000256|ARBA:ARBA00030966, ECO:0000256|HAMAP-Rule:MF_00653};
GN Name=pqqB {ECO:0000256|HAMAP-Rule:MF_00653};
GN OrderedLocusNames=Csal_0845 {ECO:0000313|EMBL:ABE58202.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58202.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE58202.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
CC -!- FUNCTION: May be involved in the transport of PQQ or its precursor to
CC the periplasm. {ECO:0000256|HAMAP-Rule:MF_00653}.
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004886, ECO:0000256|HAMAP-Rule:MF_00653}.
CC -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000256|ARBA:ARBA00008481,
CC ECO:0000256|HAMAP-Rule:MF_00653}.
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DR EMBL; CP000285; ABE58202.1; -; Genomic_DNA.
DR RefSeq; WP_011506148.1; NC_007963.1.
DR AlphaFoldDB; Q1QZA6; -.
DR STRING; 290398.Csal_0845; -.
DR KEGG; csa:Csal_0845; -.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_061120_0_0_6; -.
DR OrthoDB; 9778305at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000000239; 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; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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 NCBIfam; TIGR02108; PQQ_syn_pqqB; 1.
DR PANTHER; PTHR42663:SF7; COENZYME PQQ SYNTHESIS PROTEIN B; 1.
DR PANTHER; PTHR42663; HYDROLASE C777.06C-RELATED-RELATED; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW Rule:MF_00653}; Reference proteome {ECO:0000313|Proteomes:UP000000239};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00653}.
FT DOMAIN 51..266
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 299 AA; 32408 MW; FE9333A53FDB3261 CRC64;
MYIHVLGAAA GGGLPQWNCR CDVCRLAWAG DPRVTPRTQS SLAVSADGRS WALINCAPEV
LTQIRGTPAL FPRQGKRDTP IASILLTNGD VDHVGGLLSL RESSPYRLHA TPEIHAALRD
SPVFNVLAPD HVERVEVALE ETLTLAEGLE ARIFAVPGKA ALYLEGEDPD IGSEGEATVG
VEFRVGARRA YYIPGCAAMN ERLAARLEGA DLLLFDGTLW RDDEMIRAGV GHKTGSRMGH
MSMSGETGSM AALSSLNIGR RVFVHINNTN PVLIDDSPER REARRHGWEI AHDGMELEC
//
