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 03-AUG-2022, entry version 142.
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=10.1111/j.1574-6968.2004.tb09489.x;
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:0007744|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:0007744|PDB:2W1R, ECO:0007744|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 P37554; P37554: spoVT; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P37554; -.
DR BMRB; P37554; -.
DR SMR; P37554; -.
DR DIP; DIP-46335N; -.
DR STRING; 224308.BSU00560; -.
DR PaxDb; P37554; -.
DR PRIDE; P37554; -.
DR EnsemblBacteria; CAB11832; CAB11832; BSU_00560.
DR GeneID; 64301877; -.
DR GeneID; 936975; -.
DR KEGG; bsu:BSU00560; -.
DR PATRIC; fig|224308.179.peg.56; -.
DR eggNOG; COG2002; Bacteria.
DR OMA; IGEMGAF; -.
DR PhylomeDB; P37554; -.
DR BioCyc; BSUB:BSU00560-MON; -.
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 Pfam; PF04014; MazE_antitoxin; 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;
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:0007829|PDB:2W1T"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2W1T"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:2W1T"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2W1T"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2W1T"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:2W1T"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:2W1R"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2W1R"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 127..140
FT /evidence="ECO:0007829|PDB:2W1R"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:2W1R"
FT HELIX 159..172
FT /evidence="ECO:0007829|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
