YVDP_BACSU
ID YVDP_BACSU Reviewed; 447 AA.
AC O06997; Q795H3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Uncharacterized FAD-linked oxidoreductase YvdP;
DE EC=1.21.-.-;
DE AltName: Full=Spore coat protein YvdP;
GN Name=yvdP; OrderedLocusNames=BSU34520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Denizot F.;
RL Submitted (APR-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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12562816; DOI=10.1128/jb.185.4.1443-1454.2003;
RA Lai E.-M., Phadke N.D., Kachman M.T., Giorno R., Vazquez S., Vazquez J.A.,
RA Maddock J.R., Driks A.;
RT "Proteomic analysis of the spore coats of Bacillus subtilis and Bacillus
RT anthracis.";
RL J. Bacteriol. 185:1443-1454(2003).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Spore coat {ECO:0000269|PubMed:12562816}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; Z94043; CAB08045.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15457.1; -; Genomic_DNA.
DR PIR; G70034; G70034.
DR RefSeq; NP_391332.1; NC_000964.3.
DR RefSeq; WP_003228217.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O06997; -.
DR SMR; O06997; -.
DR IntAct; O06997; 2.
DR STRING; 224308.BSU34520; -.
DR PaxDb; O06997; -.
DR PRIDE; O06997; -.
DR EnsemblBacteria; CAB15457; CAB15457; BSU_34520.
DR GeneID; 936442; -.
DR KEGG; bsu:BSU34520; -.
DR PATRIC; fig|224308.179.peg.3739; -.
DR eggNOG; COG0277; Bacteria.
DR InParanoid; O06997; -.
DR OMA; FPQRSSH; -.
DR PhylomeDB; O06997; -.
DR BioCyc; BSUB:BSU34520-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; Sporulation.
FT CHAIN 1..447
FT /note="Uncharacterized FAD-linked oxidoreductase YvdP"
FT /id="PRO_0000360487"
FT DOMAIN 29..201
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 447 AA; 50085 MW; 1096092D325229DB CRC64;
MGSTQLTGRV IFKGDPGYTE AIKNWNPYVD VYPLVFVFAQ NSYDVSNAIK WARENKVPLR
VRSGRHALDK NLSVVSGGIV IDVSDMNKVF LDEENAIATV QTGIPVGPLV KGLARDGFMA
PFGDSPTVGI GGITMGGGFG VLSRSIGLIS DNLLALKTVD AKGRIIHADQ SHNEDLLWAS
RGGGGGNFGY NTQYTFKVHR APKTATVFNI IWPWEQLETV FKAWQKWAPF VDERLGCYLE
IYSKINGLCH AEGIFLGSKT ELIRLLKPLL HAGTPTEADI KTLYYPDAID FLDPDEPIPG
RNDQSVKFSS AWGHDFWSDE PISIMRKFLE DATGTEANFF FINWGGAISR VPKDETAFFW
RHPLFYTEWT ASWKNKSQED SNLASVERVR QLMQPYVAGS YVNVPDQNIE NFGKEYYGAN
FARLREIKAK YDPENVFRFP QSIPPSR