ID Q5Y5R9_BACLI Unreviewed; 257 AA.
AC Q5Y5R9;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Stage 0 sporulation protein A {ECO:0000256|ARBA:ARBA00015699};
DE Flags: Fragment;
GN Name=spo0A {ECO:0000313|EMBL:AAU01519.1};
OS Bacillus licheniformis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402 {ECO:0000313|EMBL:AAU01519.1};
RN [1] {ECO:0000313|EMBL:AAU01519.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G {ECO:0000313|EMBL:AAU01519.1};
RX PubMed=16943008; DOI=10.1016/j.fm.2005.05.003;
RA Rueckert A., Ronimus R.S., Morgan H.W.;
RT "Development of a real-time PCR assay targeting the sporulation gene,
RT spo0A, for the enumeration of thermophilic bacilli in milk powder.";
RL Food Microbiol. 23:220-230(2006).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR002937-1};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR002937-1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AY672769; AAU01519.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5Y5R9; -.
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 CDD; cd17561; REC_Spo0A; 1.
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 Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR002937-1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR002937-1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 5..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 125..149
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:0000256|PIRSR:PIRSR002937-1"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 257
FT /evidence="ECO:0000313|EMBL:AAU01519.1"
SQ SEQUENCE 257 AA; 28458 MW; ACCCD11D232837CA CRC64;
MEKIKVCVAD DNRELVGLLS EYIEGQSDME VLGVAYNGQE CLSLFKDKEP DVLVLDIIMP
HLDGLAVLER LRESQLKKQP NVIMLTAFGQ EDVTKKAVDL GASYFILKPF DMENLVGHIR
QVSGNGSQLT HRAPSSQSSV LRPQPESPKK NLDASITTII HEIGVPAHIK GYLYLREAIS
MVYNDIELLG SITKVLYPDI AKKFNTTASR VERAIRHAIE VAWSRGNIDS ISSLFGYTVS
MSKAKPTNSD GRDVADK
//
