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Database: UniProt
Entry: A0A1H5SW91_9FIRM
LinkDB: A0A1H5SW91_9FIRM
Original site: A0A1H5SW91_9FIRM 
ID   A0A1H5SW91_9FIRM        Unreviewed;       235 AA.
AC   A0A1H5SW91;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN05216537_103164 {ECO:0000313|EMBL:SEF54744.1};
OS   Lachnospira multipara.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospira.
OX   NCBI_TaxID=28051 {ECO:0000313|EMBL:SEF54744.1, ECO:0000313|Proteomes:UP000236726};
RN   [1] {ECO:0000313|EMBL:SEF54744.1, ECO:0000313|Proteomes:UP000236726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D15d {ECO:0000313|EMBL:SEF54744.1,
RC   ECO:0000313|Proteomes:UP000236726};
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; FNUL01000003; SEF54744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5SW91; -.
DR   Proteomes; UP000236726; 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; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000313|EMBL:SEF54744.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236726}.
FT   DOMAIN          2..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   235 AA;  28062 MW;  536CF7668A88D3C5 CRC64;
     MRILICDDNK TICDEIRNIL YELIDFEELV IDVIYTYKEL REKISYSYDL IFVDIELGRD
     KGFEAIEFLR NKYNNYRTSV VYISAYTNYA MRLFATNPLD FLLKPIKFQD IENIINKYIK
     LYKSVGKIFE YNRNKSSVYV NTRDISYFES MARKVIIHFL GGGEEIIYSS MKSIVNNEAL
     NEFVYVHQSY FVNYWMIKKF SSQEITLSDD RVIPISSQKK KDALKKYIEI SEKYK
//
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