ID SP0A_BACPU Reviewed; 191 AA.
AC P52933;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 13-SEP-2023, entry version 113.
DE RecName: Full=Stage 0 sporulation protein A;
DE Flags: Fragment;
GN Name=spo0A;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PB4;
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; U09975; AAA18876.1; -; Unassigned_DNA.
DR PIR; S60873; S60873.
DR AlphaFoldDB; P52933; -.
DR SMR; P52933; -.
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; 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 Pfam; PF00072; Response_reg; 1.
DR Pfam; PF08769; Spo0A_C; 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 3: Inferred from homology;
KW Activator; Calcium; Cytoplasm; DNA-binding; Phosphoprotein; Repressor;
KW Sporulation; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN <1..>191
FT /note="Stage 0 sporulation protein A"
FT /id="PRO_0000081231"
FT DOMAIN <1..60
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 136..155
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 191
SQ SEQUENCE 191 AA; 21288 MW; D211F2C695F56B44 CRC64;
LAVLERLREN NEMTKQPSVI MLTAFGQEDV TKKAVDLGAS YFILKPFDME NLVGHIRQVS
GNGTQVTHRS SSIQNSVLRN KPPEPKRKNL DASITTIIHE IGVPAHIKGY LYLREAISMV
YNDIELLGSI TKVLYPDIAK KFNTTASRVE RAIRHAIEVA WSRGNIDSIS SLFGYTVSMS
KAKPTNSEFI A
//
