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 03-AUG-2022, entry version 171.
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.
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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 AlphaFoldDB; P06534; -.
DR SMR; P06534; -.
DR STRING; 224308.BSU24220; -.
DR jPOST; P06534; -.
DR PaxDb; P06534; -.
DR PRIDE; P06534; -.
DR EnsemblBacteria; CAB14353; CAB14353; BSU_24220.
DR GeneID; 64304212; -.
DR GeneID; 938655; -.
DR KEGG; bsu:BSU24220; -.
DR PATRIC; fig|224308.179.peg.2639; -.
DR eggNOG; COG0745; Bacteria.
DR OMA; TKELYPM; -.
DR PhylomeDB; P06534; -.
DR BioCyc; BSUB:BSU24220-MON; -.
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:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
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 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;
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 REGION 126..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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:0007829|PDB:1LQ1"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1LQ1"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:1LQ1"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:1LQ1"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:1LQ1"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:1LQ1"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:1LQ1"
FT HELIX 249..262
FT /evidence="ECO:0007829|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
