DPAA_BACSU
ID DPAA_BACSU Reviewed; 297 AA.
AC Q04809;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Dipicolinate synthase subunit A;
DE Short=DPA synthase subunit A;
DE EC=1.3.1.-;
DE AltName: Full=Spore dipicolinate synthase subunit A;
DE AltName: Full=Stage V sporulation protein FA;
GN Name=dpaA; Synonyms=spoVFA; OrderedLocusNames=BSU16730; ORFNames=orfY;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NADP.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of dipicolinate synthase, A chain, from Bacillus
RT subtilis.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Together with DpaB, 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, ECO:0000269|Ref.4}.
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 heat-sensitive spores devoid of DPA, which can be cured by
CC supplementation with dipicolinate. {ECO:0000269|PubMed:8345520}.
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DR EMBL; L08471; AAA22381.1; -; Genomic_DNA.
DR EMBL; Z22554; CAA80274.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13546.1; -; Genomic_DNA.
DR PIR; G46665; G46665.
DR RefSeq; NP_389555.1; NC_000964.3.
DR RefSeq; WP_003231888.1; NZ_JNCM01000035.1.
DR PDB; 2RIR; X-ray; 2.79 A; A/B/C/D/E/F/G/H=2-296.
DR PDBsum; 2RIR; -.
DR AlphaFoldDB; Q04809; -.
DR SMR; Q04809; -.
DR STRING; 224308.BSU16730; -.
DR PaxDb; Q04809; -.
DR PRIDE; Q04809; -.
DR DNASU; 939652; -.
DR EnsemblBacteria; CAB13546; CAB13546; BSU_16730.
DR GeneID; 939652; -.
DR KEGG; bsu:BSU16730; -.
DR PATRIC; fig|224308.179.peg.1815; -.
DR eggNOG; COG1052; Bacteria.
DR OMA; MMAIQHT; -.
DR PhylomeDB; Q04809; -.
DR BioCyc; BSUB:BSU16730-MON; -.
DR BioCyc; MetaCyc:MON-6566; -.
DR EvolutionaryTrace; Q04809; -.
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 InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR014215; Dipicolinic_acid_synth_A.
DR InterPro; IPR031629; DpaA_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF16924; DpaA_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02853; spore_dpaA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome; Sporulation.
FT CHAIN 1..297
FT /note="Dipicolinate synthase subunit A"
FT /id="PRO_0000072083"
FT BINDING 164..165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 242..244
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 264..267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2RIR"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 126..146
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:2RIR"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:2RIR"
FT HELIX 273..294
FT /evidence="ECO:0007829|PDB:2RIR"
SQ SEQUENCE 297 AA; 31948 MW; 634B14D514B041B9 CRC64;
MLTGLKIAVI GGDARQLEII RKLTEQQADI YLVGFDQLDH GFTGAVKCNI DEIPFQQIDS
IILPVSATTG EGVVSTVFSN EEVVLKQDHL DRTPAHCVIF SGISNAYLEN IAAQAKRKLV
KLFERDDIAI YNSIPTVEGT IMLAIQHTDY TIHGSQVAVL GLGRTGMTIA RTFAALGANV
KVGARSSAHL ARITEMGLVP FHTDELKEHV KDIDICINTI PSMILNQTVL SSMTPKTLIL
DLASRPGGTD FKYAEKQGIK ALLAPGLPGI VAPKTAGQIL ANVLSKLLAE IQAEEGK
