ID M1LV21_9CLOT Unreviewed; 234 AA.
AC M1LV21;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=vanR3 {ECO:0000313|EMBL:AGF56950.1};
GN ORFNames=Cspa_c31890 {ECO:0000313|EMBL:AGF56950.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF56950.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF56950.1, 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; AGF56950.1; -; Genomic_DNA.
DR RefSeq; WP_015393268.1; NZ_AOIF01000070.1.
DR AlphaFoldDB; M1LV21; -.
DR STRING; 36745.CLSAP_29960; -.
DR KEGG; csr:Cspa_c31890; -.
DR PATRIC; fig|931276.5.peg.3211; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_9; -.
DR OrthoDB; 9790442at2; -.
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:SF2; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 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 5..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 135..233
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 135..233
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 234 AA; 27049 MW; 1A149D4264AB6E6D CRC64;
MNLYNVLIVE DEKEICDGIE IYLKNQGYNV FKAGNGLEGL EIIENEAIHL AVVDIMMPKM
DGTTMVMKLR ENYEFPVIML TAKSEEMDKI MGLNIGADDY VTKPFNPMEL LARVNSQLRR
YSKYLNVINN LEENSNSYVI GGLELNLDTK EVLLDGEDIK VTPIEFKILK LLMKNPGRVF
SAEEIYELVW KEHAINTDTV MVHVRNIREK IEIDRKNPKY LKVVWGVGYK IERQ
//
