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Database: UniProt
Entry: A0A0F2JAT7_9FIRM
LinkDB: A0A0F2JAT7_9FIRM
Original site: A0A0F2JAT7_9FIRM 
ID   A0A0F2JAT7_9FIRM        Unreviewed;       467 AA.
AC   A0A0F2JAT7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=UF75_4303 {ECO:0000313|EMBL:KJR45314.1};
OS   Desulfosporosinus sp. I2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR45314.1, ECO:0000313|Proteomes:UP000033442};
RN   [1] {ECO:0000313|EMBL:KJR45314.1, ECO:0000313|Proteomes:UP000033442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I2 {ECO:0000313|EMBL:KJR45314.1,
RC   ECO:0000313|Proteomes:UP000033442};
RA   Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.;
RL   Submitted (FEB-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:KJR45314.1}.
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DR   EMBL; JYNH01000121; KJR45314.1; -; Genomic_DNA.
DR   RefSeq; WP_045576316.1; NZ_JYNH01000121.1.
DR   AlphaFoldDB; A0A0F2JAT7; -.
DR   PATRIC; fig|1617025.3.peg.4545; -.
DR   OrthoDB; 9803970at2; -.
DR   Proteomes; UP000033442; 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   CDD; cd00156; REC; 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:SF123; NITROGEN ASSIMILATION REGULATORY PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000033442};
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   467 AA;  52346 MW;  F2C3E9A790624D10 CRC64;
     MAEAKGSILV ADDEESVRNL LSRVLTKMDY MVTTAANGEE VLAKIKGQGF DLLIMDIRMP
     KLDGMEAFKV LRLDHPSLPI IMMTAFSTVE TTLETMRLGA FDYLTKPFDV PDVKTLVEKV
     FSSRLEKDSM NLEPKTTIAP HIKAFVGSSP LMQDVFKTIG KVSASDSSVL IQGESGTGKE
     LVARTLHQYS QRKNMPFVTV NCGAIPEGVL ESEFFGHEKG AFTGAYNRKT GKFEYANGGT
     IFLDEIGEMS PPLQVKLLRV LQEREFERVG GNEKIVADVR IVAATNKSLR QSISEKTFRA
     DLFYRLNVVS IVIPPLRKRK EDIPLLAAYF RDKYCAKLNK EPKKISNEAL QVLQEYDWPG
     NVRELENIIE HAIVMGNGQV ILIEDLPMEI LLTENKKSLH TPDVNSKQGT LREMVKALEK
     DAIAVALKKT EGNKLRTAKL LDISRRALQY KIEEYGLENG ENNDEQI
//
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