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Database: UniProt
Entry: A0A0F2PLG7_9FIRM
LinkDB: A0A0F2PLG7_9FIRM
Original site: A0A0F2PLG7_9FIRM 
ID   A0A0F2PLG7_9FIRM        Unreviewed;       455 AA.
AC   A0A0F2PLG7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=VR67_00410 {ECO:0000313|EMBL:KJS14246.1};
OS   Peptococcaceae bacterium BRH_c8a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS14246.1, ECO:0000313|Proteomes:UP000033493};
RN   [1] {ECO:0000313|EMBL:KJS14246.1, ECO:0000313|Proteomes:UP000033493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS14246.1};
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:KJS14246.1}.
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DR   EMBL; LADP01000002; KJS14246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PLG7; -.
DR   STRING; 1629715.VR67_00410; -.
DR   PATRIC; fig|1629715.3.peg.1737; -.
DR   Proteomes; UP000033493; 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; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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; PS00676; SIGMA54_INTERACT_2; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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          7..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          145..374
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         56
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   455 AA;  51103 MW;  E05D0CF3BA7A7EE5 CRC64;
     MFSLSKLVLV VDDEQSVREA LRDILEDNGY QVNSASNGRE GLEMIDRLNP VAVLLDIRMP
     EMDGIKALEI INQRGSKVPV ILMTAYGSTE TTIEGMRLGA FDYLMKPLKV NEILDSLRKA
     AEIKEMLAQT RHEDPNHPKV KSNIMIGNSP IMQNIYKTIG RVSNSTATVL IRGDSGTGKE
     LVAQAIHENS VRKGNKFVKI NCASIPENLL ESELFGHEKG AFTGAVAFKQ GKFELAHKGT
     IFLDEIGEMS LTIQAKLLRV LQEREFERVG GTETIRINVR IVAATNKNLE RSIEEGTFRE
     DLYYRINVVE VLLPPLKERR EDIPALINHI IKSCSHEYNK PINGFTREAQ AILESYDWPG
     NIRELKNICV RAVLMSCGPL LTVDDLPLGL RKNSRRVEWL GEIQGDSLKE IVAEVEREVI
     LKALEENNWN RSATAQALKV NRSSLYAKMK ELGII
//
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