ID A0A0U5NUB5_9CLOT Unreviewed; 250 AA.
AC A0A0U5NUB5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=BN3456_00930 {ECO:0000313|EMBL:CUX26710.1};
OS Clostridium sp. C105KSO13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX26710.1, ECO:0000313|Proteomes:UP000198973};
RN [1] {ECO:0000313|EMBL:CUX26710.1, ECO:0000313|Proteomes:UP000198973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX26710.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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}.
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DR EMBL; FBWL01000155; CUX26710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5NUB5; -.
DR STRING; 1776045.BN3456_00930; -.
DR OrthoDB; 1769137at2; -.
DR Proteomes; UP000198973; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor 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 CDD; cd17536; REC_YesN-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR PANTHER; PTHR42713; HISTIDINE KINASE-RELATED; 1.
DR PANTHER; PTHR42713:SF3; TRANSCRIPTIONAL REGULATORY PROTEIN HPTR; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000198973}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 151..249
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 250 AA; 28499 MW; 139D7F9AC84EF6D9 CRC64;
MYKVVLIDDE PVILEGMTRG MNWEKWNCQV VGTAGSGKEG LELIEKEKPH IVFTDIAMAQ
MDGLTMLAGI KAQYDQMQVC ILTGYRDFDY AQKAIRLGVA RFLLKPSKMD ELEEAMEVMT
GRLKEHQPAE LLEGTKKKDI LNSPANNFIV KNALVYIKEN YREKLKLSDV AEHTYVSQWH
LSKLLNRQTG KSFSDILNNT RIDKAKELLK DPSLRIGDIA EEVGFLDIAH FSRVFKKITG
ISANEYRNKI
//
