ID D1PQW4_9FIRM Unreviewed; 234 AA.
AC D1PQW4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SUBVAR_06791 {ECO:0000313|EMBL:EFB74979.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB74979.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB74979.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB74979.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFB74979.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACBY02000052; EFB74979.1; -; Genomic_DNA.
DR RefSeq; WP_007048142.1; NZ_GG704770.1.
DR AlphaFoldDB; D1PQW4; -.
DR STRING; 411471.SUBVAR_06791; -.
DR GeneID; 78307372; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_2_9; -.
DR OrthoDB; 1839448at2; -.
DR Proteomes; UP000003438; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 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 DNA-binding {ECO:0000313|EMBL:EFB74979.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 131..229
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 234 AA; 26469 MW; 78BBD7BF07E03D36 CRC64;
MLQIAVVDDE REQRTLLEDC LHRYERENGV SFGIVSCGDA QEFLRQDPGG FDIVLLDIQM
PGLDGMAAAR QLREQNRRLV LIFITNMAQF AIEGYAVDAM DFILKPVSYY RLAASLTKAR
GRLQTEAGVA LVLHTKDGTY HLDSARVHYI EMFNHHTIFH TEDGVFDTTG SLKKLEEQLA
GQSFARCNNG YLVNLRYVRG VEGSDVVVAG DRLLISRTRR KAFLQRMSEY FGGQ
//
