ID A0A136WHA7_9FIRM Unreviewed; 242 AA.
AC A0A136WHA7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=yehT_1 {ECO:0000313|EMBL:KXL53729.1};
GN ORFNames=CLNEO_09550 {ECO:0000313|EMBL:KXL53729.1};
OS Anaerotignum neopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL53729.1, ECO:0000313|Proteomes:UP000070539};
RN [1] {ECO:0000313|EMBL:KXL53729.1, ECO:0000313|Proteomes:UP000070539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL53729.1,
RC ECO:0000313|Proteomes:UP000070539};
RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL Submitted (JAN-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}.
CC -!- FUNCTION: Required for high-level post-exponential phase expression of
CC a series of secreted proteins. {ECO:0000256|ARBA:ARBA00037164}.
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:KXL53729.1}.
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DR EMBL; LRVM01000002; KXL53729.1; -; Genomic_DNA.
DR RefSeq; WP_066085416.1; NZ_LRVM01000002.1.
DR AlphaFoldDB; A0A136WHA7; -.
DR STRING; 36847.CLNEO_09550; -.
DR OrthoDB; 9802383at2; -.
DR Proteomes; UP000070539; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR CDD; cd00156; REC; 1.
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:SF3; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000070539}.
FT DOMAIN 3..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 134..233
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 242 AA; 28302 MW; 85ADAEC76B2DE7D7 CRC64;
MLRIAICDDD QFICSEIEKM ILSYKKEFYI KVEIDVFFSG ERLIHFIQNE HSYDLIFLDI
ELGTITGVDV GRQIRNGFDD HLSKIVFISA KTGYEMELFD VQPMNFLKKP IDKEKLLGYL
KLAAKIIEKE NKYFEYQTQQ TINKVNFQDI LYLESKLKKV KIVTVQGNDF FNGSLEKTIQ
LLPPIFVRSH GSFVVNFNHI EKISKDEIVM TNGQAIPVSR RYFKRLQEVQ LEIAKEIKNA
NL
//
