(data stored in ACNUC7421 zone)

SWISSPROT: SPOVT_BACSU

ID   SPOVT_BACSU             Reviewed;         178 AA.
AC   P37554;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 129.
DE   RecName: Full=Stage V sporulation protein T {ECO:0000305};
GN   Name=spoVT {ECO:0000303|PubMed:8755877}; Synonyms=yabL;
GN   OrderedLocusNames=BSU00560;
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;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8755877; DOI=10.1128/jb.178.15.4500-4507.1996;
RA   Bagyan I., Hobot J., Cutting S.M.;
RT   "A compartmentalized regulator of developmental gene expression in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 178:4500-4507(1996).
RN   [4]
RP   SUBUNIT, DOMAIN, AND DNA-BINDING.
RX   PubMed=15063493; DOI=10.1016/j.femsle.2004.02.013;
RA   Dong T.C., Cutting S.M., Lewis R.J.;
RT   "DNA-binding studies on the Bacillus subtilis transcriptional regulator and
RT   AbrB homologue, SpoVT.";
RL   FEMS Microbiol. Lett. 233:247-256(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22522895; DOI=10.1128/jb.00504-12;
RA   Ramirez-Peralta A., Stewart K.A., Thomas S.K., Setlow B., Chen Z., Li Y.Q.,
RA   Setlow P.;
RT   "Effects of the SpoVT regulatory protein on the germination and germination
RT   protein levels of spores of Bacillus subtilis.";
RL   J. Bacteriol. 194:3417-3425(2012).
RN   [6] {ECO:0000244|PDB:2RO5}
RP   STRUCTURE BY NMR OF 1-55.
RX   PubMed=19000822; DOI=10.1016/j.str.2008.08.014;
RA   Sullivan D.M., Bobay B.G., Kojetin D.J., Thompson R.J., Rance M.,
RA   Strauch M.A., Cavanagh J.;
RT   "Insights into the nature of DNA binding of AbrB-like transcription
RT   factors.";
RL   Structure 16:1702-1713(2008).
RN   [7] {ECO:0000244|PDB:2W1R, ECO:0000244|PDB:2W1T}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX   PubMed=18996130; DOI=10.1016/j.jmb.2008.10.061;
RA   Asen I., Djuranovic S., Lupas A.N., Zeth K.;
RT   "Crystal structure of SpoVT, the final modulator of gene expression during
RT   spore development in Bacillus subtilis.";
RL   J. Mol. Biol. 386:962-975(2009).
CC   -!- FUNCTION: Transcriptional factor that regulates positively or
CC       negatively the expression of a large number of forespore-specific sigma
CC       G-dependent genes. May provide a mechanism of feedback control that is
CC       important for forespore development (PubMed:8755877). SpoVT levels
CC       during spore formation have a major impact on the germination and the
CC       resistance of the resultant spores (PubMed:22522895).
CC       {ECO:0000269|PubMed:22522895, ECO:0000269|PubMed:8755877}.
CC   -!- SUBUNIT: Homotetramer (PubMed:18996130) (Probable). Two monomers
CC       dimerize via their N-terminal swapped-hairpin domains. These dimers
CC       further associate into tetramers through helical interactions between
CC       their C-terminal GAF-like domains (PubMed:18996130).
CC       {ECO:0000269|PubMed:18996130, ECO:0000305|PubMed:15063493}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-15739529, EBI-15739529;
CC   -!- INDUCTION: Expression is regulated by the sporulation transcription
CC       factor sigma G. {ECO:0000269|PubMed:8755877}.
CC   -!- DOMAIN: The N-terminal domain binds DNA non-specifically and the C-
CC       terminal GAF-like domain is crucial to its correct folding and
CC       function. The non-specific DNA-binding activity of the N-terminal
CC       domain is modulated by the C-terminal domain, which perhaps in
CC       combination with another unknown factor, confers activity and
CC       specificity. {ECO:0000269|PubMed:15063493,
CC       ECO:0000269|PubMed:18996130}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to aberrantly formed
CC       spores (PubMed:8755877). Mutant spores release their dipicolinic acid
CC       (DPA) via germinant receptor (GR)-dependent germination more rapidly
CC       than wild-type spores. Spores are also more sensitive to UV radiation
CC       and outgrow slowly (PubMed:22522895). {ECO:0000269|PubMed:22522895,
CC       ECO:0000269|PubMed:8755877}.
CC   -!- SIMILARITY: To B.subtilis AbrB and Abh. {ECO:0000305}.
DR   EMBL; D26185; BAA05291.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11832.1; -; Genomic_DNA.
DR   PIR; F69716; F69716.
DR   RefSeq; NP_387937.1; NC_000964.3.
DR   RefSeq; WP_003218365.1; NZ_JNCM01000028.1.
DR   PDB; 2RO5; NMR; -; A/B=1-55.
DR   PDB; 2W1R; X-ray; 1.50 A; A=56-178.
DR   PDB; 2W1T; X-ray; 2.60 A; A/B=1-178.
DR   PDBsum; 2RO5; -.
DR   PDBsum; 2W1R; -.
DR   PDBsum; 2W1T; -.
DR   SMR; P37554; -.
DR   DIP; DIP-46335N; -.
DR   STRING; 224308.BSU00560; -.
DR   PaxDb; P37554; -.
DR   PRIDE; P37554; -.
DR   EnsemblBacteria; CAB11832; CAB11832; BSU00560.
DR   GeneID; 936975; -.
DR   KEGG; bsu:BSU00560; -.
DR   PATRIC; fig|224308.179.peg.56; -.
DR   eggNOG; ENOG4108M14; Bacteria.
DR   eggNOG; COG2002; LUCA.
DR   HOGENOM; HOG000197058; -.
DR   KO; K04769; -.
DR   OMA; GEMGAFA; -.
DR   PhylomeDB; P37554; -.
DR   BioCyc; BSUB:BSU00560-MONOMER; -.
DR   EvolutionaryTrace; P37554; -.
DR   PRO; PR:P37554; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR014213; SpoVT.
DR   InterPro; IPR007159; SpoVT-AbrB_dom.
DR   InterPro; IPR037914; SpoVT-AbrB_sf.
DR   InterPro; IPR039472; SpoVT_GAF.
DR   Pfam; PF04014; MazE_antitoxin; 1.
DR   Pfam; PF15714; SpoVT_C; 1.
DR   PIRSF; PIRSF026579; Spore_V_T; 1.
DR   SMART; SM00966; SpoVT_AbrB; 1.
DR   SUPFAM; SSF89447; SSF89447; 1.
DR   TIGRFAMs; TIGR01439; lp_hng_hel_AbrB; 1.
DR   TIGRFAMs; TIGR02851; spore_V_T; 1.
DR   PROSITE; PS51740; SPOVT_ABRB; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37554.
DR   SWISS-2DPAGE; P37554.
KW   3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW   Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..178
FT                   /note="Stage V sporulation protein T"
FT                   /id="PRO_0000072088"
FT   DOMAIN          5..51
FT                   /note="SpoVT-AbrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT   REGION          56..178
FT                   /note="GAF-like"
FT                   /evidence="ECO:0000305|PubMed:18996130"
FT   STRAND          6..9
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   STRAND          14..17
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   HELIX           20..25
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   STRAND          33..38
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   STRAND          44..48
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   HELIX           51..54
FT                   /evidence="ECO:0000244|PDB:2W1T"
FT   HELIX           58..70
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          72..77
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          79..88
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   HELIX           90..93
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   HELIX           100..108
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          112..116
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          118..123
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          127..140
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   STRAND          143..155
FT                   /evidence="ECO:0000244|PDB:2W1R"
FT   HELIX           159..172
FT                   /evidence="ECO:0000244|PDB:2W1R"
SQ   SEQUENCE   178 AA;  19742 MW;  19418022DD371180 CRC64;
     MKATGIVRRI DDLGRVVIPK EIRRTLRIRE GDPLEIFVDR DGEVILKKYS PISELGDFAK
     EYADALYDSL GHSVLICDRD VYIAVSGSSK KDYLNKSISE MLERTMDQRS SVLESDAKSV
     QLVNGIDEDM NSYTVGPIVA NGDPIGAVVI FSKDQTMGEV EHKAVETAAG FLARQMEQ
//

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