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Database: UniProt
Entry: G2SYX0_ROSHA
LinkDB: G2SYX0_ROSHA
Original site: G2SYX0_ROSHA 
ID   G2SYX0_ROSHA            Unreviewed;       235 AA.
AC   G2SYX0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   OrderedLocusNames=RHOM_16375 {ECO:0000313|EMBL:AEN98379.1};
OS   Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN98379.1, ECO:0000313|Proteomes:UP000008178};
RN   [1] {ECO:0000313|EMBL:AEN98379.1, ECO:0000313|Proteomes:UP000008178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC   {ECO:0000313|Proteomes:UP000008178};
RX   PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA   Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT   "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL   Genome Announc. 3:E0128615-E0128615(2015).
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; CP003040; AEN98379.1; -; Genomic_DNA.
DR   RefSeq; WP_009860887.1; NC_015977.1.
DR   AlphaFoldDB; G2SYX0; -.
DR   STRING; 585394.RHOM_16375; -.
DR   GeneID; 77460802; -.
DR   KEGG; rho:RHOM_16375; -.
DR   eggNOG; COG3279; Bacteria.
DR   HOGENOM; CLU_000445_14_2_9; -.
DR   OrthoDB; 9779387at2; -.
DR   BioCyc; RHOM585394:G1H02-3250-MONOMER; -.
DR   Proteomes; UP000008178; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008178}.
FT   DOMAIN          3..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          130..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   235 AA;  27976 MW;  FD401DFF2D1066B1 CRC64;
     MLNIAVCDDS RTDVEMLESA FDKLVQYQFS YEVYFTAKEL LKHVIDDGEM YHLYIFDIEM
     PEMNGLQLAK EIRKIDAKAL FVFLTGYTQY VMDVFEVITF DYISKPITVE KLESVLLKAM
     QYLHMIKRDF VFQFRKNQFR ISCDDIVYFE KKGRQAVIHT ISENFKANMT TEEIWKQLDD
     KVFAHIHVSY IINLGHIRAI EGDEVVMDNE ERLLIARSHK QNLKEKHMEF VRRMV
//
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