ID A0A371AW59_9FIRM Unreviewed; 514 AA.
AC A0A371AW59;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=DWV06_08090 {ECO:0000313|EMBL:RDU23807.1};
OS Anaerosacchariphilus polymeriproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerosacchariphilus.
OX NCBI_TaxID=1812858 {ECO:0000313|EMBL:RDU23807.1, ECO:0000313|Proteomes:UP000255036};
RN [1] {ECO:0000313|EMBL:RDU23807.1, ECO:0000313|Proteomes:UP000255036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCWD5 {ECO:0000313|EMBL:RDU23807.1,
RC ECO:0000313|Proteomes:UP000255036};
RA Kim W., Yang S.-H., Oh J., Lee J.-H., Kwon K.K.;
RT "Anaerosacharophilus polymeroproducens gen. nov. sp. nov., an anaerobic
RT bacterium isolated from salt field.";
RL Submitted (JUL-2018) 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:RDU23807.1}.
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DR EMBL; QRCT01000019; RDU23807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371AW59; -.
DR OrthoDB; 9794370at2; -.
DR Proteomes; UP000255036; 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; 1.
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, ECO:0000313|EMBL:RDU23807.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000255036}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 412..510
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 514 AA; 60202 MW; CBE8CBF779507809 CRC64;
MYTVLIADDE KVIREGLSCI INWTDYGFTI CGEASNGEET LNLILKKQPN LVLLDINMPK
LYGINVIKLA RDRGYQGKFI ILSGYSDFKY AQSAIKLGVN EYLTKPIDED ELSRSIESIK
TTLISEAQNL ENIFQYKQKA KNTILHELIT ESSSLSLNDI QYIHLYADKY QILLYENYSY
KFRDVSYDFA DILRLTNTSN LFDYFIEDNM NVILLKGDVA LKKFNRFLEH YDRIPQKGSP
LDSIFIAYGR PVNHIFDISI SYKEAAALIK RRFFCKKGQH TLGFPDFPAI ETKNIMITRE
IIEEYAFELA DYIQCFNRQK VNDSLIHLEN HLYNVRNNIS ETKLFLADLY LLIKERINRL
YSNIQIPFPT NSEIIQLIQS KFYLYEIIQF YSSQFEMIMN ALGAYSRNSI LEDILYYIEH
NFHNHIKLET IAPLFGYNSA YLGKLIHKTV GKNFNSYLDE IRIEHSKKLL SQQELKVYEI
AECIGYNNVD YFHKKFKKYV GMSPAEYRKS MKEG
//
