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SP0A_BACAN
ID   SP0A_BACAN              Reviewed;         264 AA.
AC   P52928; Q6HTL2; Q6KMV2; Q81M59;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Stage 0 sporulation protein A;
GN   Name=spo0A; OrderedLocusNames=BA_4394, GBAA_4394, BAS4076;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-214.
RC   STRAIN=UM23-C1;
RX   PubMed=7885226; DOI=10.1111/j.1365-2958.1994.tb02176.x;
RA   Brown D.P., Ganova-Raeva L., Green B.D., Wilkinson S.R., Young M.,
RA   Youngman P.;
RT   "Characterization of spo0A homologues in diverse Bacillus and Clostridium
RT   species identifies a probable DNA-binding domain.";
RL   Mol. Microbiol. 14:411-426(1994).
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) (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT56377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016879; AAP28110.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33514.2; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56377.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U09970; AAA18871.1; -; Genomic_DNA.
DR   PIR; S60868; S60868.
DR   RefSeq; NP_846624.1; NC_003997.3.
DR   RefSeq; WP_003161566.1; NZ_QPKQ01000004.1.
DR   AlphaFoldDB; P52928; -.
DR   SMR; P52928; -.
DR   STRING; 260799.BAS4076; -.
DR   DNASU; 1087648; -.
DR   EnsemblBacteria; AAP28110; AAP28110; BA_4394.
DR   EnsemblBacteria; AAT33514; AAT33514; GBAA_4394.
DR   GeneID; 45024055; -.
DR   KEGG; ban:BA_4394; -.
DR   KEGG; bar:GBAA_4394; -.
DR   KEGG; bat:BAS4076; -.
DR   PATRIC; fig|198094.11.peg.4363; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_072509_0_0_9; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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:0051606; P:detection of stimulus; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
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   3: Inferred from homology;
KW   Activator; Calcium; Cytoplasm; DNA-binding; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repressor; Sporulation; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..264
FT                   /note="Stage 0 sporulation protein A"
FT                   /id="PRO_0000081226"
FT   DOMAIN          5..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        196..215
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
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   CONFLICT        22
FT                   /note="Y -> C (in Ref. 4; AAA18871)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   264 AA;  29440 MW;  62F8155B55739D63 CRC64;
     MEKIKVCLVD DNKELVSMLE SYVAAQDDME VIGTAYNGQE CLNLLKDKQP DVLVLDIIMP
     HLDGLAVLEK MRHIERLRQP SVIMLTAFGQ EDVTKKAVDL GASYFILKPF DMENLTSHIR
     QVSGKANATI KRPLPSFRSA TTVDGKPKNL DASITSIIHE IGVPAHIKGY MYLREAISMV
     YNDIELLGSI TKVLYPDIAK KYNTTASRVE RAIRHAIEVA WSRGNIDSIS SLFGYTVSMS
     KAKPTNSEFI AMVADKLRLE HKAS
 
 
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