ID A0A0J1G7V9_9FIRM Unreviewed; 411 AA.
AC A0A0J1G7V9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=RHS_2318 {ECO:0000313|EMBL:KLU71604.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71604.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU71604.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU71604.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU71604.1}.
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DR EMBL; JNGB01000020; KLU71604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G7V9; -.
DR PATRIC; fig|1504536.3.peg.2673; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17536; REC_YesN-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR041522; CdaR_GGDEF.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR PANTHER; PTHR42713; HISTIDINE KINASE-RELATED; 1.
DR PANTHER; PTHR42713:SF3; TRANSCRIPTIONAL REGULATORY PROTEIN HPTR; 1.
DR Pfam; PF17853; GGDEF_2; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 306..404
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 411 AA; 47070 MW; 9D359735E6009A30 CRC64;
MYGILIVDDE PMICEGLKAF ADRWDYSFET VLTARNGEEA LAVIAKESPQ ILITDIRMPK
MDGVELLQRI RELKMDIHVI VLSGYDDFEY VRAMAVLGIE NYLLKPVSHE ELGQTLKIVI
KHLDQERNLK MKAQLDINLI RENIINRWMY GSIGENELQE RADFLELDLE AASYQPCILR
LLGKDMKREI ELKNQIHRIC VSILSERCVC YYSRNYDGDT IVVFCRNEEE KDQLPIIQAI
NQCVEMVLNE LQVKLYVLLG SPAEDYWKVA DSFAKAVAGG IYLDKIPNES VGDDPEESSN
SSPFSLRLAN YVLEHYEEDL SLKSLAQHFR GNAAYIGQIF KRDIGRSFSD YLKEIRIEKA
KELLKKGNSS AKEISAKVGF QNTTYFCAVF KKETGVSPAE YKKIFGENAR L
//
