SP0A_GEOSE
ID SP0A_GEOSE Reviewed; 259 AA.
AC P52934;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Stage 0 sporulation protein A;
GN Name=spo0A;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RC STRAIN=B4419;
RX PubMed=10089466; DOI=10.1107/s0907444998012682;
RA Muchova K., Lewis R.J., Brannigan J.A., Offen W.A., Brown D.P., Barak I.,
RA Youngman P., Wilkinson A.J.;
RT "Crystallization of the regulatory and effector domains of the key
RT sporulation response regulator Spo0A.";
RL Acta Crystallogr. D 55:671-676(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-209.
RC STRAIN=B4419;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-130, AND PHOSPHORYLATION AT
RP ASP-55.
RX PubMed=10556024; DOI=10.1006/jmbi.1999.3261;
RA Lewis R.J., Brannigan J.A., Muchova K., Barak I., Wilkinson A.J.;
RT "Phosphorylated aspartate in the structure of a response regulator
RT protein.";
RL J. Mol. Biol. 294:9-15(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-130.
RX PubMed=10731426; DOI=10.1006/jmbi.2000.3598;
RA Lewis R.J., Muchova K., Brannigan J.A., Barak I., Leonard G.,
RA Wilkinson A.J.;
RT "Domain swapping in the sporulation response regulator Spo0A.";
RL J. Mol. Biol. 297:757-770(2000).
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;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by KinA and KinB. {ECO:0000250}.
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DR EMBL; AJ002297; CAA05307.1; -; Genomic_DNA.
DR EMBL; U09977; AAA18878.1; -; Unassigned_DNA.
DR PIR; S60875; S60875.
DR RefSeq; WP_033016446.1; NZ_RCTK01000026.1.
DR PDB; 1DZ3; X-ray; 1.65 A; A=1-130.
DR PDB; 1FC3; X-ray; 2.00 A; A/B/C=140-259.
DR PDB; 1QMP; X-ray; 2.00 A; A/B/C/D=1-130.
DR PDBsum; 1DZ3; -.
DR PDBsum; 1FC3; -.
DR PDBsum; 1QMP; -.
DR AlphaFoldDB; P52934; -.
DR SMR; P52934; -.
DR GeneID; 58573819; -.
DR EvolutionaryTrace; P52934; -.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Calcium; Cytoplasm; DNA-binding; Metal-binding;
KW Phosphoprotein; Repressor; Sporulation; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..259
FT /note="Stage 0 sporulation protein A"
FT /id="PRO_0000081233"
FT DOMAIN 4..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 191..210
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:10556024"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:1DZ3"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:1DZ3"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1DZ3"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1DZ3"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:1DZ3"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1DZ3"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1FC3"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:1FC3"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1FC3"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:1FC3"
SQ SEQUENCE 259 AA; 28970 MW; 99836A6E6242749C CRC64;
MSIKVCIADD NRELVSLLDE YISSQPDMEV IGTAYNGQDC LQMLEEKRPD ILLLDIIMPH
LDGLAVLERI RAGFEHQPNV IMLTAFGQED VTKKAVELGA SYFILKPFDM ENLAHHIRQV
YGKTTPVVRK AAPAPQVRDN KPKNLDASIT SIIHEIGVPA HIKGYLYLRE AIAMVYHDIE
LLGSITKVLY PDIAKKYNTT ASRVERAIRH AIEVAWSRGN LESISSLFGY TVSVSKAKPT
NSEFIAMVAD KLRLEHKAS
