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Database: UniProt
Entry: A0A0F2Q9H3_9CLOT
LinkDB: A0A0F2Q9H3_9CLOT
Original site: A0A0F2Q9H3_9CLOT 
ID   A0A0F2Q9H3_9CLOT        Unreviewed;       250 AA.
AC   A0A0F2Q9H3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=VR72_06145 {ECO:0000313|EMBL:KJS22370.1};
OS   Clostridiaceae bacterium BRH_c20a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX   NCBI_TaxID=1629719 {ECO:0000313|EMBL:KJS22370.1, ECO:0000313|Proteomes:UP000033488};
RN   [1] {ECO:0000313|EMBL:KJS22370.1, ECO:0000313|Proteomes:UP000033488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c20a {ECO:0000313|EMBL:KJS22370.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS22370.1}.
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DR   EMBL; LADT01000018; KJS22370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2Q9H3; -.
DR   STRING; 1629719.VR72_06145; -.
DR   Proteomes; UP000033488; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   DOMAIN          8..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..249
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   250 AA;  28879 MW;  55ACEF086A06EAE4 CRC64;
     MMEIKEITVI VAEDEPALRQ KIIAILEEVP EIEVICEAEN GIQLIEQCLI HEPDAVFADI
     GLPEMSGMEA VQNLFTDLPD LFAVFITAYS QYAVEAFEIS AVDYVLKPVT GKRILKAVAK
     LKQHMLEKEA LRKQRNISNI KKEKIPVRDE NGLIFLNQDE IFMLEKEQKR TIIHTKTHVY
     KTLATINSLK QKLNGSFFQT HRSFIVNLDK VHKIFPLGDR TNMIEFEDYD KQAQVSRNNL
     AELYRKLEFE
//
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