ID   SP0A_NIACI              Reviewed;         210 AA.
AC   P52931;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Stage 0 sporulation protein A;
DE   Flags: Fragment;
GN   Name=spo0A;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4513 / DSM 11 / BCRC 10605 / CCUG 7416 / JCM 2504 / NBRC 13626
RC   / NCIMB 9374 / NCTC 2610;
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}.
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DR   EMBL; U09973; AAA18874.1; -; Genomic_DNA.
DR   PIR; S60871; S60871.
DR   AlphaFoldDB; P52931; -.
DR   SMR; P52931; -.
DR   STRING; 1397.ABW02_06390; -.
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   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   Repressor; Sporulation; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..>210
FT                   /note="Stage 0 sporulation protein A"
FT                   /id="PRO_0000081228"
FT   DOMAIN          5..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        192..>210
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   NON_TER         210
SQ   SEQUENCE   210 AA;  23689 MW;  D75EF1CE5FB32456 CRC64;
     MKKIKVCIVD DNRELVGLLE EYIDAQDDME VIGVAHNGQE CLELVEQLEP DVMVLDIIMP
     HIDGLAVLER MRQMNKPMPN VIMLTAFGQE DVTKKAVELG ASYFILKPFD MEYLASHIRQ
     VSGKTTGFVR KSSSSFKTQE PKTKNLDASI TSIIHEIGVP AHIKGYLYLR EAISMVYNDI
     ELLGSITKVL YPDIAKKYNT TASRVERAIR