ID A0A1M6DEM5_PSEXY Unreviewed; 229 AA.
AC A0A1M6DEM5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02745725_00945 {ECO:0000313|EMBL:SHI71448.1};
OS Pseudobutyrivibrio xylanivorans DSM 14809.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1123012 {ECO:0000313|EMBL:SHI71448.1, ECO:0000313|Proteomes:UP000184185};
RN [1] {ECO:0000313|EMBL:SHI71448.1, ECO:0000313|Proteomes:UP000184185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14809 {ECO:0000313|EMBL:SHI71448.1,
RC ECO:0000313|Proteomes:UP000184185};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYQ01000004; SHI71448.1; -; Genomic_DNA.
DR RefSeq; WP_072913425.1; NZ_FQYQ01000004.1.
DR AlphaFoldDB; A0A1M6DEM5; -.
DR STRING; 185007.SAMN02910350_00121; -.
DR OrthoDB; 9790442at2; -.
DR Proteomes; UP000184185; 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:SF26; 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:UP000184185};
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 130..229
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 130..229
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 229 AA; 26254 MW; 364DA63F4EE3BC65 CRC64;
MSRILIIEDE EAIAELEKDY LELSNFEVDI EGDGEKGLQK ALAGNYDMYI LDLMLPGIDG
FELCKRIREV KNVPILMVTA KKEEIDKIRG LGLGADDYIT KPFSPSELVA RVKAHLSRYE
RLVQSPNIQK DEISIRGLRI DKASRRVWIN GEEKIFTAKE FDLLAFLAEN PNVIYSKEQL
FETLWGEESI GDISTVTVHV NKIREKIELN TSKPQYIETI WGVGYRFKV
//