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Database: UniProt
Entry: A0A1Q8QH84_9FIRM
LinkDB: A0A1Q8QH84_9FIRM
Original site: A0A1Q8QH84_9FIRM 
ID   A0A1Q8QH84_9FIRM        Unreviewed;       474 AA.
AC   A0A1Q8QH84;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=DSOL_4861 {ECO:0000313|EMBL:OLN26707.1};
OS   Desulfosporosinus metallidurans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN26707.1, ECO:0000313|Proteomes:UP000186102};
RN   [1] {ECO:0000313|EMBL:OLN26707.1, ECO:0000313|Proteomes:UP000186102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL {ECO:0000313|EMBL:OLN26707.1,
RC   ECO:0000313|Proteomes:UP000186102};
RA   Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT   "Complete genome of Desulfosporosinus sp. OL.";
RL   Submitted (SEP-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}.
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:OLN26707.1}.
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DR   EMBL; MLBF01000071; OLN26707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8QH84; -.
DR   STRING; 1888891.DSOL_4861; -.
DR   Proteomes; UP000186102; 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   Reference proteome {ECO:0000313|Proteomes:UP000186102};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          25..139
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          162..389
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   MOD_RES         74
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   474 AA;  52888 MW;  6802A5E78446670A CRC64;
     MVVSWLKSNI LNIVIILREV ERVRRILVAD DEANMRWVLE RALTKAGYEV ETVEDGQLAL
     DRALAERPDL VLVDLKMPKM DGLSVLHILK ERYPDLLIVM MTAHGSTTTA VEAMKAGAQD
     YLMKPFDIDE LLITVAKAFE VESLREQVDY LKGGAQHGGW QLVGDSEEIQ AVKHLAERVA
     PTPATVLIQG ESGTGKELVA QAIHTLSPRV DGPFIRVNCA ALTENLLESE LFGHEKGAFT
     GAHARKTGRF ELADSGTLFL DEIAELSFNV QAKLLRVLQE RTFERVGGEK TIKVDVRIIA
     ATNRDLLKEA QEGRFREDLY YRLNVFPISV PPLRERREDI SLLTEHFLGK FRTYGGSKTL
     GPGVLSHLMA YTWPGNVREL ENVVERMVII SQGVVIGMDS LPLFDTSSKL AKNPGSFVLP
     PEGVSLEEIE KSFLHQAMEQ TGGNQSQAAK RLGLSRHAFL YRLEKYGIDP HWGI
//
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