SP0A_PRIMG
ID SP0A_PRIMG Reviewed; 212 AA.
AC P52932;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Stage 0 sporulation protein A;
DE Flags: Fragment;
GN Name=spo0A;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35985 / VT1660;
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; U09974; AAA18875.1; -; Genomic_DNA.
DR PIR; S60872; S60872.
DR AlphaFoldDB; P52932; -.
DR SMR; P52932; -.
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_0000081230"
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; 23862 MW; 8E3395AE21358F57 CRC64;
MKKIKVCLVD DNRELIGLLE DYISEQEDME VIGVAYNGQE CLSILKDKNP DVLVLDIIMP
HLDGLAVLGQ LKEMKKENYP NVIMLTAFGQ EDVTKKAVDL GAAYFILKPF DMENLVNHIR
QVSGQTSSFM QRSSSSMRSH RDSKPANLDA SITSIIHEIG VPAHIKGYLY LREAISMVYK
DIELLGSITK VLYPDIAKKY NTTASRVERA IR