ID A0A1I5RTH6_9FIRM Unreviewed; 234 AA.
AC A0A1I5RTH6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN05216343_11087 {ECO:0000313|EMBL:SFP61571.1};
OS Oscillibacter sp. PC13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillibacter.
OX NCBI_TaxID=1855299 {ECO:0000313|EMBL:SFP61571.1, ECO:0000313|Proteomes:UP000198573};
RN [1] {ECO:0000313|EMBL:SFP61571.1, ECO:0000313|Proteomes:UP000198573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC13 {ECO:0000313|EMBL:SFP61571.1,
RC ECO:0000313|Proteomes:UP000198573};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOXE01000010; SFP61571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RTH6; -.
DR STRING; 1855299.SAMN05216343_11087; -.
DR OrthoDB; 152576at2; -.
DR Proteomes; UP000198573; Unassembled WGS sequence.
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:SF85; RESPONSE REGULATOR SAER; 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:UP000198573};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 127..225
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 127..225
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 234 AA; 26887 MW; D09C26CCCD408BAC CRC64;
MGRNILVVED DHNISDLIHM YLVKEGFDVR IAGDGGKAIE EFQKQVPDLI LLDIMLPVMD
GWSVCAKIRE TSKVPIIMLT AKSEVFDRIQ GLEMGADDYI VKPFEMKELI ARINAVLRRT
EIPNDTTKRL TFDKLVIDLD SYELIVDGKK IDTPPKELEL LYHLASTPNR VYTRNQLLDE
VWGFDYFGDS RTVDVHIKRL REKVENVSDQ WALKTVWGVG YKFELGAQQT EKSN
//