(data stored in SCRATCH zone)

SWISSPROT: SP0A_BACSU

ID   SP0A_BACSU              Reviewed;         267 AA.
AC   P06534; P70990;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   11-DEC-2019, entry version 162.
DE   RecName: Full=Stage 0 sporulation protein A;
DE   AltName: Full=Stage 0 sporulation protein C;
DE   AltName: Full=Stage 0 sporulation protein G;
GN   Name=spo0A; Synonyms=spo0C, spo0G; OrderedLocusNames=BSU24220;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3921963; DOI=10.1073/pnas.82.9.2665;
RA   Kudoh J., Ikeuchi T., Kurahashi K.;
RT   "Nucleotide sequences of the sporulation gene spo0A and its mutant genes of
RT   Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2665-2668(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3018427; DOI=10.1007/bf00422059;
RA   Ikeuchi T., Kudoh J., Tsunasawa S.;
RT   "Amino-terminal structure of spoOA protein and sequence homology with spoOF
RT   and spoOB proteins.";
RL   Mol. Gen. Genet. 203:371-376(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3157992; DOI=10.1073/pnas.82.9.2647;
RA   Ferrari F.A., Trach K.A., Le Coq D., Spence J., Ferrari E., Hoch J.A.;
RT   "Characterization of the spo0A locus and its deduced product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2647-2651(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RC   STRAIN=168 / JH642;
RX   PubMed=9044256; DOI=10.1046/j.1365-2958.1997.2091573.x;
RA   Oke V., Shchepetov M., Cutting S.;
RT   "SpoIVB has two distinct functions during spore formation in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 23:223-230(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX   PubMed=3151993; DOI=10.1099/00221287-134-12-3249;
RA   Shoji K., Hiratsuka S., Kawamura F., Kobayashi Y.;
RT   "New suppressor mutation sur0B of spo0B and spo0F mutations in Bacillus
RT   subtilis.";
RL   J. Gen. Microbiol. 134:3249-3257(1988).
RN   [8]
RP   MUTAGENESIS OF ASN-12; PRO-60; ALA-87 AND GLN-90.
RX   PubMed=2121995; DOI=10.1016/s0022-2836(05)80357-2;
RA   Olmedo G., Gottlin Ninfa E., Stock J., Youngman P.;
RT   "Novel mutations that alter the regulation of sporulation in Bacillus
RT   subtilis. Evidence that phosphorylation of regulatory protein SpoOA
RT   controls the initiation of sporulation.";
RL   J. Mol. Biol. 215:359-372(1990).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 148-267.
RX   PubMed=12176382; DOI=10.1016/s0969-2126(02)00803-1;
RA   Zhao H., Msadek T., Zapf J., Madhusudan X., Hoch J.A., Varughese K.I.;
RT   "DNA complexed structure of the key transcription factor initiating
RT   development in sporulating bacteria.";
RL   Structure 10:1041-1050(2002).
CC   -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC       be an element of the effector pathway responsible for the activation of
CC       sporulation genes in response to nutritional stress. Spo0A may act in
CC       concert with Spo0H (a sigma factor) to control the expression of some
CC       genes that are critical to the sporulation process. Repressor of abrB,
CC       activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3'
CC       (0A box).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by KinA and KinB.
CC   -!- MISCELLANEOUS: Stage 0 mutants lack the ability to form the asymmetric
CC       septum characteristic of the initiation of the sporulation process.
DR   EMBL; M10082; AAA22786.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12581.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14353.1; -; Genomic_DNA.
DR   EMBL; U68235; AAC44872.1; -; Genomic_DNA.
DR   EMBL; M23656; AAA22842.1; -; Genomic_DNA.
DR   PIR; A94036; SZBS0A.
DR   RefSeq; NP_390302.1; NC_000964.3.
DR   RefSeq; WP_003226427.1; NZ_JNCM01000036.1.
DR   PDB; 1LQ1; X-ray; 2.30 A; A/B/C/D=148-267.
DR   PDBsum; 1LQ1; -.
DR   SMR; P06534; -.
DR   STRING; 224308.BSU24220; -.
DR   PaxDb; P06534; -.
DR   PRIDE; P06534; -.
DR   EnsemblBacteria; CAB14353; CAB14353; BSU24220.
DR   GeneID; 938655; -.
DR   KEGG; bsu:BSU24220; -.
DR   PATRIC; fig|224308.179.peg.2639; -.
DR   eggNOG; ENOG4107QQR; Bacteria.
DR   eggNOG; COG0784; LUCA.
DR   HOGENOM; HOG000057639; -.
DR   KO; K07699; -.
DR   OMA; TKELYPM; -.
DR   PhylomeDB; P06534; -.
DR   BioCyc; BSUB:BSU24220-MONOMER; -.
DR   EvolutionaryTrace; P06534; -.
DR   PRO; PR:P06534; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008356; P:asymmetric cell division; IGI:UniProtKB.
DR   GO; GO:0090529; P:cell septum assembly; IGI:UniProtKB.
DR   GO; GO:0051606; P:detection of stimulus; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0045881; P:positive regulation of sporulation resulting in formation of a cellular spore; IGI:UniProtKB.
DR   GO; GO:0090606; P:single-species surface biofilm formation; IMP:CACAO.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR014879; Spo0A_C.
DR   InterPro; IPR012052; Spore_0_A.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF08769; Spo0A_C; 1.
DR   PIRSF; PIRSF002937; Res_reg_Spo0A; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   TIGRFAMs; TIGR02875; spore_0_A; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P06534.
DR   SWISS-2DPAGE; P06534.
KW   3D-structure; Activator; Calcium; Cytoplasm; DNA-binding; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repressor; Sporulation; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..267
FT                   /note="Stage 0 sporulation protein A"
FT                   /id="PRO_0000081234"
FT   DOMAIN          5..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        199..218
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   METAL           10
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   METAL           11
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   METAL           56
FT                   /note="Calcium"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         12
FT                   /note="N->S: In SOF-1 mutant."
FT                   /evidence="ECO:0000269|PubMed:2121995"
FT   MUTAGEN         60
FT                   /note="P->S: In COI-1 mutant."
FT                   /evidence="ECO:0000269|PubMed:2121995"
FT   MUTAGEN         87
FT                   /note="A->V: In COI-2 and COI-12 mutants."
FT                   /evidence="ECO:0000269|PubMed:2121995"
FT   MUTAGEN         90
FT                   /note="Q->K: In COI-15 mutant."
FT                   /evidence="ECO:0000269|PubMed:2121995"
FT   HELIX           153..164
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           171..185
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           187..191
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   TURN            193..196
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           197..204
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           209..225
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           231..235
FT                   /evidence="ECO:0000244|PDB:1LQ1"
FT   HELIX           249..262
FT                   /evidence="ECO:0000244|PDB:1LQ1"
SQ   SEQUENCE   267 AA;  29691 MW;  2F4943A5A5061DD9 CRC64;
     MEKIKVCVAD DNRELVSLLS EYIEGQEDME VIGVAYNGQE CLSLFKEKDP DVLVLDIIMP
     HLDGLAVLER LRESDLKKQP NVIMLTAFGQ EDVTKKAVDL GASYFILKPF DMENLVGHIR
     QVSGNASSVT HRAPSSQSSI IRSSQPEPKK KNLDASITSI IHEIGVPAHI KGYLYLREAI
     SMVYNDIELL GSITKVLYPD IAKKFNTTAS RVERAIRHAI EVAWSRGNID SISSLFGYTV
     SMTKAKPTNS EFIAMVADKL RLEHKAS
//

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