ID M1MSP1_9CLOT Unreviewed; 231 AA.
AC M1MSP1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=ycbL {ECO:0000313|EMBL:AGF54597.1};
GN ORFNames=Cspa_c08200 {ECO:0000313|EMBL:AGF54597.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF54597.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF54597.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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; CP004121; AGF54597.1; -; Genomic_DNA.
DR RefSeq; WP_015390923.1; NZ_AOIF01000144.1.
DR AlphaFoldDB; M1MSP1; -.
DR STRING; 36745.CLSAP_08600; -.
DR KEGG; csr:Cspa_c08200; -.
DR PATRIC; fig|931276.5.peg.776; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_3_9; -.
DR OrthoDB; 9803564at2; -.
DR Proteomes; UP000011728; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17574; REC_OmpR; 1.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 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; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF40; SENSORY TRANSDUCTION PROTEIN REGX3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000011728};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 126..226
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 126..226
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 231 AA; 26287 MW; 78D90144B8241D8A CRC64;
MKHIFFVEDN LSLINGLSFA IKKQGYEIDV ARTILEAEAL LVNKKYDLVI LDVSLPDGCG
YDLCKKIRKT SKVPIIFLTA ADEETDIIMG LDIGGDDYIT KPFKLAVFMS KINALLRRSD
NFIQADTELN SNGINVQLLK GEVYKNGEQL DLTTSEYKVL CLFMENPHIV LSPEQILSKL
WDCNENYIDN NTITVYIRRL RTKIEDNPSE PQKIVTVRRM GYKWNTVDGG V
//