YKUV_BACSU
ID YKUV_BACSU Reviewed; 148 AA.
AC O31699; O31403;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thiol-disulfide oxidoreductase YkuV;
DE EC=1.8.-.-;
GN Name=ykuV; OrderedLocusNames=BSU14230;
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 Scanlan E., Devine K.M.;
RT "Sequence of the Bacillus subtilis chromosome from ykuA to cse-15.";
RL Submitted (NOV-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 SEQUENCE REVISION TO 59 AND C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP STRUCTURE BY NMR OF REDUCED AND OXIDIZED FORMS, DISULFIDE BOND, AND
RP CHARACTERIZATION.
RX PubMed=16418167; DOI=10.1074/jbc.m512015200;
RA Zhang X., Hu Y., Guo X., Lescop E., Li Y., Xia B., Jin C.;
RT "The Bacillus subtilis ykuV is a thiol:disulfide oxidoreductase revealed by
RT its redox structures and activity.";
RL J. Biol. Chem. 281:8296-8304(2006).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AJ222587; CAA10885.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13296.2; -; Genomic_DNA.
DR PIR; C69867; C69867.
DR RefSeq; NP_389306.2; NC_000964.3.
DR RefSeq; WP_003245810.1; NZ_JNCM01000035.1.
DR PDB; 2B5X; NMR; -; A=1-148.
DR PDB; 2B5Y; NMR; -; A=1-148.
DR PDBsum; 2B5X; -.
DR PDBsum; 2B5Y; -.
DR AlphaFoldDB; O31699; -.
DR BMRB; O31699; -.
DR SMR; O31699; -.
DR STRING; 224308.BSU14230; -.
DR PaxDb; O31699; -.
DR PRIDE; O31699; -.
DR EnsemblBacteria; CAB13296; CAB13296; BSU_14230.
DR GeneID; 938804; -.
DR KEGG; bsu:BSU14230; -.
DR PATRIC; fig|224308.179.peg.1552; -.
DR eggNOG; COG0526; Bacteria.
DR InParanoid; O31699; -.
DR OMA; EYVPAYY; -.
DR PhylomeDB; O31699; -.
DR BioCyc; BSUB:BSU14230-MON; -.
DR EvolutionaryTrace; O31699; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Electron transport;
KW Oxidoreductase; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..148
FT /note="Thiol-disulfide oxidoreductase YkuV"
FT /id="PRO_0000233105"
FT DOMAIN 2..145
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 41..44
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:16418167"
FT CONFLICT 144..148
FT /note="LAETE -> WLKRNRYLTK (in Ref. 1; CAA10885)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2B5X"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2B5X"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2B5X"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:2B5X"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2B5X"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2B5X"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2B5Y"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2B5X"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:2B5X"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2B5X"
SQ SEQUENCE 148 AA; 17017 MW; 2D67230FFCFD3077 CRC64;
MKLRQPMPEL TGEKAWLNGE VTREQLIGEK PTLIHFWSIS CHLCKEAMPQ VNEFRDKYQD
QLNVVAVHMP RSEDDLDPGK IKETAAEHDI TQPIFVDSDH ALTDAFENEY VPAYYVFDKT
GQLRHFQAGG SGMKMLEKRV NRVLAETE
