ID R4FZD9_9BACI Unreviewed; 244 AA.
AC R4FZD9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Stage 0 sporulation protein A {ECO:0000256|ARBA:ARBA00015699, ECO:0000256|PIRNR:PIRNR002937};
GN ORFNames=KN10_0150 {ECO:0000313|EMBL:GAC89714.1};
OS Anoxybacillus flavithermus NBRC 109594.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1315967 {ECO:0000313|EMBL:GAC89714.1, ECO:0000313|Proteomes:UP000013057};
RN [1] {ECO:0000313|Proteomes:UP000013057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109594 {ECO:0000313|Proteomes:UP000013057};
RA Matsutani M., Shirakihara Y., Imada K., Yakushi T., Matsushita K.;
RT "Draft Genome Sequence of a Thermophilic Member of the Bacillaceae,
RT Anoxybacillus flavithermus Strain Kn10, Isolated from the Kan-nawa Hot
RT Spring in Japan.";
RL Genome Announc.1:e00311-13(2013).
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). {ECO:0000256|ARBA:ARBA00025691}.
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.
CC {ECO:0000256|PIRNR:PIRNR002937}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR002937}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAC89714.1}.
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DR EMBL; BARH01000001; GAC89714.1; -; Genomic_DNA.
DR AlphaFoldDB; R4FZD9; -.
DR Proteomes; UP000013057; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
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-UniRule.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR02875; spore_0_A; 1.
DR PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
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; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|PIRNR:PIRNR002937};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002937};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR002937};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002937};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002937,
KW ECO:0000256|PIRSR:PIRSR002937-1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR002937};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|PIRNR:PIRNR002937};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR002937};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR002937};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|PIRNR:PIRNR002937}.
FT DOMAIN 1..107
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT MOD_RES 41
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 244 AA; 27330 MW; B2B9CD388CB5866E CRC64;
MHLLEEYITS QGDMEVIGVA YNGQDCLQLL RDRDPDVLVL DIIMPHLDGL AVLEKLRIIK
QPLPNVIMLT AFGQEDVTKK AVELGASYFI LKPFDIEHLV NQIRHVCGKK PAVFKRPLLA
PIRDGKPKNL DASITNIIHE IGVPAHIKGY LYLREAIAMV YNDVELLGSI TKVLYPDIAK
KYNTTASRVE RAIRHAIEVA WSRGNLESIS SLFGHTVSMS KAKPTNSEFI AMVADRLRLE
HKAS
//
