ID Q2RGH8_MOOTA Unreviewed; 252 AA.
AC Q2RGH8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=Moth_2172 {ECO:0000313|EMBL:ABC20461.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC20461.1};
RN [1] {ECO:0000313|EMBL:ABC20461.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC20461.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000232; ABC20461.1; -; Genomic_DNA.
DR RefSeq; YP_431004.1; NC_007644.1.
DR AlphaFoldDB; Q2RGH8; -.
DR STRING; 264732.Moth_2172; -.
DR EnsemblBacteria; ABC20461; ABC20461; Moth_2172.
DR KEGG; mta:Moth_2172; -.
DR PATRIC; fig|264732.11.peg.2366; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_1_9; -.
DR OrthoDB; 9809318at2; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR CDD; cd17532; REC_LytTR_AlgR-like; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR046947; LytR-like.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR37299:SF1; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR PANTHER; PTHR37299; TRANSCRIPTIONAL REGULATOR-RELATED; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00850; LytTR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 145..251
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 252 AA; 29047 MW; B31E27E65200B9C0 CRC64;
MTLKALIVDD EYPARQELRF MLQEFKDIEV VGEATNARET LNLVSALDYT ILFLDINMPG
MNGLELSRAI QKRPNPPFII FVTAYEEYAL QAFEVNAVDY LLKPFDEKRL RQAIDKVRRL
VEQRQQPAVP AGEAAHGGKG RLNRLPVEKE GKTILLDQDD LIYACTQGDN VYLKTSTDQY
LTRFTLKELE SRLDPRSFFR CHRCYIVNLN RVRELVPFFN GTYTLIMADK QQSEVPVSRN
QARKLKSLLG IN
//
