ID   YNEN_BACSU              Reviewed;         170 AA.
AC   O31820;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Thioredoxin-like protein YneN;
GN   Name=yneN; OrderedLocusNames=BSU18010;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / 1A1;
RX   PubMed=15342593; DOI=10.1128/jb.186.18.6230-6238.2004;
RA   Erlendsson L.S., Moeller M., Hederstedt L.;
RT   "Bacillus subtilis StoA is a thiol-disulfide oxidoreductase important for
RT   spore cortex synthesis.";
RL   J. Bacteriol. 186:6230-6238(2004).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: No sporulation-related phenotype.
CC       {ECO:0000269|PubMed:15342593}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13685.1; -; Genomic_DNA.
DR   PIR; E69891; E69891.
DR   RefSeq; NP_389684.1; NC_000964.3.
DR   RefSeq; WP_003244797.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31820; -.
DR   SMR; O31820; -.
DR   STRING; 224308.BSU18010; -.
DR   PaxDb; O31820; -.
DR   PRIDE; O31820; -.
DR   EnsemblBacteria; CAB13685; CAB13685; BSU_18010.
DR   GeneID; 938193; -.
DR   KEGG; bsu:BSU18010; -.
DR   PATRIC; fig|224308.179.peg.1962; -.
DR   eggNOG; COG0526; Bacteria.
DR   InParanoid; O31820; -.
DR   OMA; RYVGEPQ; -.
DR   PhylomeDB; O31820; -.
DR   BioCyc; BSUB:BSU18010-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Membrane; Redox-active center;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..170
FT                   /note="Thioredoxin-like protein YneN"
FT                   /id="PRO_0000386532"
FT   TRANSMEM        5..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          33..170
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        71..74
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   170 AA;  19372 MW;  D32B262EAB715760 CRC64;
     MLKKWLAGIL LIMLVGYTGW NLYQTYSKKE VGIQEGQQAP DFSLKTLSGE KSSLQDAKGK
     KVLLNFWATW CKPCRQEMPA MEKLQKEYAD KLAVVAVNFT SAEKSEKQVR AFADTYDLTF
     PILIDKKGIN ADYNVMSYPT TYILDEKGVI QDIHVGTMTK KEMEQKLDLD