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Database: UniProt
Entry: A0A101VQ72_9FIRM
LinkDB: A0A101VQ72_9FIRM
Original site: A0A101VQ72_9FIRM 
ID   A0A101VQ72_9FIRM        Unreviewed;       243 AA.
AC   A0A101VQ72;
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_09335 {ECO:0000313|EMBL:KUO58663.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO58663.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO58663.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO58663.1};
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:KUO58663.1}.
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DR   EMBL; LOEZ01000085; KUO58663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101VQ72; -.
DR   STRING; 1734398.APF84_09335; -.
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   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 2.40.50.1020; LytTr DNA-binding domain; 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          3..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          134..234
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         60
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   243 AA;  28216 MW;  97CBE754D16E159E CRC64;
     MLNIAICDDL HSDRMQMEKL TRSFCIEEDH DINIIKFENG EKLLHYFVHE KAAFDIVFLD
     IYMSGINGLK SAEQIRKYDS DCKIIFTTSS TEHSLESFKV FPFNYLVKPI TKAIFNPVVK
     KAVKDISEEK QKSLAIKIGS NIQTIFYKEI LFIESRAKTV NINTIDHGIF STKSKLDDIQ
     VQMNAKRFLR CHKSFLVNMD FISSVEDYTF KLSNGKQIPI TQRTYASVKK VFYDYVMDKA
     NLK
//
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