YDAP_BACSU
ID YDAP_BACSU Reviewed; 574 AA.
AC P96591; Q797M1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative thiamine pyrophosphate-containing protein YdaP;
GN Name=ydaP; OrderedLocusNames=BSU04340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP REGULATION.
RC STRAIN=168;
RX PubMed=10220166; DOI=10.1099/13500872-145-4-869;
RA Petersohn A., Antelmann H., Gerth U., Hecker M.;
RT "Identification and transcriptional analysis of new members of the sigmaB
RT regulon in Bacillus subtilis.";
RL Microbiology 145:869-880(1999).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000305};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000305};
CC -!- INDUCTION: Transcriptionally regulated by SigB.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB001488; BAA19271.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12241.1; -; Genomic_DNA.
DR PIR; G69769; G69769.
DR RefSeq; NP_388315.1; NC_000964.3.
DR RefSeq; WP_003246569.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P96591; -.
DR SMR; P96591; -.
DR IntAct; P96591; 1.
DR STRING; 224308.BSU04340; -.
DR PaxDb; P96591; -.
DR PRIDE; P96591; -.
DR EnsemblBacteria; CAB12241; CAB12241; BSU_04340.
DR GeneID; 938239; -.
DR KEGG; bsu:BSU04340; -.
DR PATRIC; fig|224308.179.peg.460; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; P96591; -.
DR OMA; YEATHEC; -.
DR PhylomeDB; P96591; -.
DR BioCyc; BSUB:BSU04340-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..574
FT /note="Putative thiamine pyrophosphate-containing protein
FT YdaP"
FT /id="PRO_0000380114"
FT REGION 384..464
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT COILED 28..55
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 256..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294..313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 63138 MW; F887A1271B7E9710 CRC64;
MAHKTAGQAM TELLEQWGVD HVYGIPGDSI NEFIEELRHE RNQLKFIQTR HEEVAALAAA
AEAKLTGKIG VCLSIAGPGA VHLLNGLYDA KADGAPVLAI AGQVSSGEVG RDYFQEIKLE
QMFEDVAVFN REVHSAESLP DLLNQAIRTA YSKKGVAVLS VSDDLFAEKI KREPVYTSPV
YIEGNLEPKK EQLVTCAQYI NNAKKPIILA GQGMKKAKRE LLEFADKAAA PIVVTLPAKG
VVPDKHPHFL GNLGQIGTKP AYEAMEECDL LIMLGTSFPY RDYLPDDTPA IQLDSDPAKI
GKRYPVTAGL VCDSALGLRE LTEYIERKED RRFLNACTEH MQHWWNEIEK DETEATTPLK
PQQVVARLQE AAADDAVLSV DVGTVTVWMA RHFKMNANQD FIVSSWLATM GCGLPGAIAA
SLSEPERQAI AVCGDGGFSM VMQDLPTAVK YKLPITVVIL NNENLGMIEY EQQVKGNIDY
VTKLQNVDYA AFAESCGAKG IKVTKAEELA PAFHEALHSD QPVVVDVMIG NEPPLPGKIT
YGQAKGFSKY MLKNFFENQK FEMPSLKKSL KRLF
