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Database: UniProt
Entry: A0A101W046_9FIRM
LinkDB: A0A101W046_9FIRM
Original site: A0A101W046_9FIRM 
ID   A0A101W046_9FIRM        Unreviewed;       253 AA.
AC   A0A101W046;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=APF84_14535 {ECO:0000313|EMBL:KUO63835.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO63835.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO63835.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO63835.1};
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 (OCT-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:KUO63835.1}.
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DR   EMBL; LOEZ01000044; KUO63835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101W046; -.
DR   STRING; 1734398.APF84_14535; -.
DR   Proteomes; UP000053404; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   CDD; cd17532; REC_LytTR_AlgR-like; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR046947; LytR-like.
DR   InterPro; IPR007492; LytTR_DNA-bd_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR37299:SF1; STAGE 0 SPORULATION PROTEIN A HOMOLOG; 1.
DR   PANTHER; PTHR37299; TRANSCRIPTIONAL REGULATOR-RELATED; 1.
DR   Pfam; PF04397; LytTR; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00850; LytTR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50930; HTH_LYTTR; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   DOMAIN          4..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          147..253
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   253 AA;  29365 MW;  961E29C8CD161FE4 CRC64;
     MKMRALLVDD ESPARKELRY LLQSFEDVQI VGEAENALEA LELINNVKYS VIFLDINMPG
     LNGIELARQL SERPDAPAII FTTAHEEYAF DAFSVHAYDF VLKPIHPKRL EEALQTVRER
     KKLNCPQPAK TTPSKKEYID MRPLEVIPAE QNSKTILIRP EEIIFISTDK DNVYIKTGNE
     SYLTRFTLRE LEARLDSNSF FRTHRCYLVN IRKMRELIPY FNGTYTVVVE DKERSEVPVS
     RTQARKLKEI LGI
//
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