SP0A_BREPA
ID SP0A_BREPA Reviewed; 212 AA.
AC P52929;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Stage 0 sporulation protein A;
DE Flags: Fragment;
GN Name=spo0A;
OS Brevibacillus parabrevis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB 8598
RC / IAM 1031;
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; U09971; AAA18872.1; -; Genomic_DNA.
DR AlphaFoldDB; P52929; -.
DR SMR; P52929; -.
DR STRING; 54914.AV540_04695; -.
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..>212
FT /note="Stage 0 sporulation protein A"
FT /id="PRO_0000081236"
FT DOMAIN 5..123
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 194..>212
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 212
SQ SEQUENCE 212 AA; 23843 MW; B626CD30F7400137 CRC64;
MSKIEVLLAD DNREFVSLLE EYISSQYDMN VIGVAYNGNE VVRLLQERVP DVLILDIIMP
HLDGLAVLEQ IQAMRLSPQP KIIMLTAFGQ EEITKKAVEL GAAYYILKPF DMEVLAQRIR
QIITTKPASS FVTSVKPQST LQVRGRNLDA SITSIIHEIG VPAHIKGYLY LREAITMVYN
DVELLGSITK VLYPDIAKKF NTTASHVERA IR