STOA_BACSU
ID STOA_BACSU Reviewed; 165 AA.
AC O31687;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sporulation thiol-disulfide oxidoreductase A;
DE AltName: Full=Stage IV sporulation protein H;
DE Flags: Precursor;
GN Name=stoA; Synonyms=spoIVH; OrderedLocusNames=BSU13840;
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 CATALYTIC ACTIVITY, ROLE IN SPORULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15292147; DOI=10.1128/jb.186.16.5450-5459.2004;
RA Imamura D., Kobayashi K., Sekiguchi J., Ogasawara N., Takeuchi M., Sato T.;
RT "spoIVH (ykvV), a requisite cortex formation gene, is expressed in both
RT sporulating compartments of Bacillus subtilis.";
RL J. Bacteriol. 186:5450-5459(2004).
RN [3]
RP CATALYTIC ACTIVITY, AND ROLE IN SPORULATION.
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).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=15322369; DOI=10.1271/bbb.68.1801;
RA Tanaka R., Araki Y., Mizukami M., Miyauchi A., Ishibashi M., Tokunaga H.,
RA Tokunaga M.;
RT "Expression and purification of the Bacillus subtilis thioredoxin
RT superfamily protein YkvV.";
RL Biosci. Biotechnol. Biochem. 68:1801-1804(2004).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase with a reductive function,
CC involved in spore cortex synthesis. It could be involved either in
CC breaking disulfide bonds in cortex components or in proteins that are
CC important for cortex synthesis, or in thiol/disulfide bond interchange.
CC {ECO:0000269|PubMed:15292147, ECO:0000269|PubMed:15342593}.
CC -!- SUBCELLULAR LOCATION: Spore outer membrane {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants have spores sensitive to heat, lysozyme
CC and chloroform, and in which the cortex is absent.
CC {ECO:0000269|PubMed:15292147}.
CC -!- MISCELLANEOUS: StoA and ykvU are cotranscribed under the control of
CC sigma E.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AL009126; CAB13257.1; -; Genomic_DNA.
DR PIR; E69869; E69869.
DR RefSeq; NP_389267.1; NC_000964.3.
DR RefSeq; WP_003245444.1; NZ_JNCM01000035.1.
DR PDB; 3ERW; X-ray; 2.50 A; A/B/C/D/E/F/G=22-164.
DR PDBsum; 3ERW; -.
DR AlphaFoldDB; O31687; -.
DR SMR; O31687; -.
DR STRING; 224308.BSU13840; -.
DR PaxDb; O31687; -.
DR DNASU; 936262; -.
DR EnsemblBacteria; CAB13257; CAB13257; BSU_13840.
DR GeneID; 936262; -.
DR KEGG; bsu:BSU13840; -.
DR PATRIC; fig|224308.179.peg.1508; -.
DR eggNOG; COG0526; Bacteria.
DR InParanoid; O31687; -.
DR OMA; RKMGRVH; -.
DR PhylomeDB; O31687; -.
DR BioCyc; BSUB:BSU13840-MON; -.
DR EvolutionaryTrace; O31687; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043594; C:outer endospore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; 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 InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Membrane; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal; Sporulation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..165
FT /note="Sporulation thiol-disulfide oxidoreductase A"
FT /id="PRO_0000034289"
FT DOMAIN 27..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 65..68
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3ERW"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3ERW"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3ERW"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3ERW"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3ERW"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3ERW"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3ERW"
SQ SEQUENCE 165 AA; 18807 MW; E875C09AC8000DD0 CRC64;
MLTKRLLTIY IMLLGLIAWF PGAAQAEEKQ PAVPAVFLMK TIEGEDISIP NKGQKTILHF
WTSWCPPCKK ELPQFQSFYD AHPSDSVKLV TVNLVNSEQN QQVVEDFIKA NKLTFPIVLD
SKGELMKEYH IITIPTSFLL NEKGEIEKTK IGPMTAEQLK EWTEE
