SP0A_CLOIN
ID SP0A_CLOIN Reviewed; 277 AA.
AC P52939;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Stage 0 sporulation protein A homolog;
GN Name=spo0A;
OS Clostridium innocuum.
OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelatoclostridium.
OX NCBI_TaxID=1522;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14501 / DSM 1286 / JCM 1292 / NCIB 10674 / B-3;
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 (By similarity).
CC {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}.
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DR EMBL; U09981; AAA18882.1; -; Unassigned_DNA.
DR PIR; S60879; S60879.
DR AlphaFoldDB; P52939; -.
DR SMR; P52939; -.
DR STRING; 999413.HMPREF1094_03379; -.
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 PIRSF; PIRSF002937; Res_reg_Spo0A; 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..277
FT /note="Stage 0 sporulation protein A homolog"
FT /id="PRO_0000081241"
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 199..218
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 277 AA; 31804 MW; 134F69B43D16E488 CRC64;
MNNKMNVYLV DDSMEMIHSM KEALTKSDGY QVIGSATNGE QCVNELRGKH LDVLVLDLIM
PKKDGISVLH DLKKNHIQVD HIICTTPFVN DLIVAGVQNY RIDYILMKPF EIEQLCDKLN
FIVGYTRKEH ISSNVLQVNL DDDEKERLQK LELESEITEL LHEIGIPAHI KGYMYLRTAI
LETYLNVDFL GQITKVLYPE IAKKYATTAS RVERAIRHAI EVAWNRGNID AIDDIFGYTI
SASKAKPTNS EFIAMISDKL RLEHRLRNKN NVIKTFR