ID B2A521_NATTJ Unreviewed; 280 AA.
AC B2A521;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN OrderedLocusNames=Nther_1689 {ECO:0000313|EMBL:ACB85263.1};
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB85263.1, ECO:0000313|Proteomes:UP000001683};
RN [1] {ECO:0000313|EMBL:ACB85263.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB85263.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RX PubMed=21642468; DOI=10.1128/JB.05157-11;
RA Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA Kyrpides N., Wiegel J.;
RT "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT Natranaerobius thermophilus JW/NM-WN-LF.";
RL J. Bacteriol. 193:4023-4024(2011).
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.
CC {ECO:0000256|ARBA:ARBA00024867, ECO:0000256|PIRNR:PIRNR002937}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR002937}.
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DR EMBL; CP001034; ACB85263.1; -; Genomic_DNA.
DR AlphaFoldDB; B2A521; -.
DR STRING; 457570.Nther_1689; -.
DR KEGG; nth:Nther_1689; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_072509_0_0_9; -.
DR InParanoid; B2A521; -.
DR Proteomes; UP000001683; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
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-UniRule.
DR CDD; cd17561; REC_Spo0A; 1.
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 PANTHER; PTHR44591:SF27; PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
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; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR002937};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002937};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002937};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002937};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002937,
KW ECO:0000256|PIRSR:PIRSR002937-1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001683};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR002937};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|PIRNR:PIRNR002937};
KW Transcription {ECO:0000256|PIRNR:PIRNR002937};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR002937};
KW Two-component regulatory system {ECO:0000256|PIRNR:PIRNR002937}.
FT DOMAIN 4..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 280 AA; 31718 MW; F556418B4EA7C177 CRC64;
MLIDILIVDD NKEFCEILKD YLAEHDDFNV VGTAHNGEEA IEKIKQSPPD ILLLDIIMPI
LDGIGVLEYL QKEDFENKPK TIMLTAFGHE KITQRAVSLG ADYYILKPFS MDILADRIKQ
LYSGFGMSKP EIDNLAATDD SKEMVLQDSQ NIGNSINPEN NKVDLEAEIT DIIHELGVPA
HIKGYLYLRK AIMMVIEDPD LLNSVTKILY PKIAETFETT PSRVERAIRH AIEVAWNRND
IETIKNLFGY TINTEKGKPT NSEFIAIVAD KLRLKTKQRA
//
