DPAB_BACSU
ID DPAB_BACSU Reviewed; 200 AA.
AC Q04810;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Dipicolinate synthase subunit B;
DE Short=DPA synthase subunit B;
DE EC=1.3.1.-;
DE AltName: Full=Spore dipicolinate synthase subunit B;
DE AltName: Full=Stage V sporulation protein FB;
GN Name=dpaB; Synonyms=spoVFB; OrderedLocusNames=BSU16740; ORFNames=orfX;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8098035; DOI=10.1016/s0021-9258(18)98372-9;
RA Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H.;
RT "Organization and nucleotide sequence of the Bacillus subtilis
RT diaminopimelate operon, a cluster of genes encoding the first three enzymes
RT of diaminopimelate synthesis and dipicolinate synthase.";
RL J. Biol. Chem. 268:9448-9465(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DPA SYNTHESIS, GENE NAME,
RP INDUCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=168, and SG38;
RX PubMed=8345520; DOI=10.1006/jmbi.1993.1403;
RA Daniel R.A., Errington J.;
RT "Cloning, DNA sequence, functional analysis and transcriptional regulation
RT of the genes encoding dipicolinic acid synthetase required for sporulation
RT in Bacillus subtilis.";
RL J. Mol. Biol. 232:468-483(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Together with DpaA, catalyzes the conversion of
CC dihydrodipicolinate to dipicolinate (DPA), which constitutes up to 10%
CC of the dry weight of the spore. {ECO:0000269|PubMed:8345520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-dihydrodipicolinate + NADP(+) = dipicolinate + H(+) +
CC NADPH; Xref=Rhea:RHEA:47092, ChEBI:CHEBI:15378, ChEBI:CHEBI:30620,
CC ChEBI:CHEBI:36167, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC -!- SUBUNIT: Dipicolinate synthase likely consists of DpaA and DpaB, since
CC both proteins are required for DPA synthesis.
CC {ECO:0000269|PubMed:8345520}.
CC -!- INDUCTION: Is not expressed during vegetative growth; is expressed at
CC stage 5 of sporulation specifically in the mother cell compartment,
CC under the control of the sigma-K factor. Is repressed by GerE.
CC {ECO:0000269|PubMed:8098035, ECO:0000269|PubMed:8345520}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene has no effect on
CC vegetative growth but causes a sporulation defect, characterized by
CC very low sporulation frequencies and heat-sensitive spores devoid of
CC DPA, which can be cured by supplementation with dipicolinate.
CC {ECO:0000269|PubMed:8098035, ECO:0000269|PubMed:8345520}.
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DR EMBL; L08471; AAA22382.1; -; Genomic_DNA.
DR EMBL; Z22554; CAA80275.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13547.1; -; Genomic_DNA.
DR PIR; F46665; F46665.
DR RefSeq; NP_389556.1; NC_000964.3.
DR RefSeq; WP_003244650.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q04810; -.
DR SMR; Q04810; -.
DR STRING; 224308.BSU16740; -.
DR PaxDb; Q04810; -.
DR PRIDE; Q04810; -.
DR DNASU; 939660; -.
DR EnsemblBacteria; CAB13547; CAB13547; BSU_16740.
DR GeneID; 939660; -.
DR KEGG; bsu:BSU16740; -.
DR PATRIC; fig|224308.179.peg.1816; -.
DR eggNOG; COG0452; Bacteria.
DR InParanoid; Q04810; -.
DR OMA; AKAHLRN; -.
DR PhylomeDB; Q04810; -.
DR BioCyc; BSUB:BSU16740-MON; -.
DR BioCyc; MetaCyc:MON-6567; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR014214; Dipicolinic_acid_synth_B.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR PIRSF; PIRSF001390; Dipicolinate_synth_subunit_B; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR02852; spore_dpaB; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome; Sporulation.
FT CHAIN 1..200
FT /note="Dipicolinate synthase subunit B"
FT /id="PRO_0000072084"
SQ SEQUENCE 200 AA; 21869 MW; C67BDF4089A8CAD3 CRC64;
MSSLKGKRIG FGLTGSHCTY EAVFPQIEEL VNEGAEVRPV VTFNVKSTNT RFGEGAEWVK
KIEDLTGYEA IDSIVKAEPL GPKLPLDCMV IAPLTGNSMS KLANAMTDSP VLMAAKATIR
NNRPVVLGIS TNDALGLNGT NLMRLMSTKN IFFIPFGQDD PFKKPNSMVA KMDLLPQTIE
KALMHQQLQP ILVENYQGND
