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Database: UniProt
Entry: A0A0F2SLX8_9FIRM
LinkDB: A0A0F2SLX8_9FIRM
Original site: A0A0F2SLX8_9FIRM 
ID   A0A0F2SLX8_9FIRM        Unreviewed;       458 AA.
AC   A0A0F2SLX8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=VR66_02600 {ECO:0000313|EMBL:KJS50477.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS50477.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS50477.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS50477.1};
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:KJS50477.1}.
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DR   EMBL; LADV01000027; KJS50477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2SLX8; -.
DR   PATRIC; fig|1629714.3.peg.3725; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   PANTHER; PTHR32071:SF57; SIGMA L-DEPENDENT TRANSCRIPTIONAL REGULATOR YQIR-RELATED; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..117
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          143..372
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   458 AA;  52269 MW;  69BFE61F52F92AAE CRC64;
     MARILVIDDE EGVCELLRDV LENAGYEVFV TYTAAEGMEA LNNFDPDTIL LDIKLPDDDG
     IRVMEKIKDR GFTVPIILMT AFGTTEIAIH AMKEGAHDYL NKPLNLDELI ITVQRTVKMK
     YLVSEVAILR EKLEDELNPF DNFIGQSRIM QEISKIIGRI ADTDITVLIQ GESGTGKEVV
     ARSIHKNSKR NHCPFININC ATIPENLMES ELFGHEKGSF TGAISQKMGK FELAHSGTVF
     LDEIGELTHH AQTKLLRVLQ EREFERVGGI NNIKVDIRIL AATNKDLQKL VEEGKFREDL
     FYRLNVVNIK LPPLKDRKED IILLVNYYIN KFAQKHVKKI TSMSKEALNF MINYPWPGNV
     RELINTCEQA VVMTRGTVIL PDDLAMLEGN RPSCRDSDLE LNIKLRLKRP IKDILAEVEK
     QVIIKTLKDH NWSRQESANT LGFNRRSLYA KMKEYDLL
//
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