ID U2CYU7_9FIRM Unreviewed; 254 AA.
AC U2CYU7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=HMPREF1982_04411 {ECO:0000313|EMBL:ERI89720.1};
OS Clostridiales bacterium oral taxon 876 str. F0540.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI89720.1, ECO:0000313|Proteomes:UP000016490};
RN [1] {ECO:0000313|EMBL:ERI89720.1, ECO:0000313|Proteomes:UP000016490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0540 {ECO:0000313|EMBL:ERI89720.1,
RC ECO:0000313|Proteomes:UP000016490};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERI89720.1}.
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DR EMBL; AWSZ01000078; ERI89720.1; -; Genomic_DNA.
DR AlphaFoldDB; U2CYU7; -.
DR STRING; 1321778.HMPREF1982_04411; -.
DR PATRIC; fig|1321778.3.peg.4342; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_1_9; -.
DR OrthoDB; 9809318at2; -.
DR Proteomes; UP000016490; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; 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; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 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 DNA-binding {ECO:0000313|EMBL:ERI89720.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000016490}.
FT DOMAIN 3..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 137..210
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 254 AA; 29717 MW; D1087C6AD2762E52 CRC64;
MYNILILEDD CIQLKTLSEI IKQSSDLYKV YEASNTAEAM KAALTERIDL FYIDISLKNE
SGLKFAEEIR KKEGYKLTWI VFVTIYKDYM LPAFKKIHCY DYILKPYNKE NIQQITKLLL
SDDRSQVAAT EIRENFIIVN VKNIQVKIFI NEIIFVEVFI RTSIIHTING SFTIDYLSLK
KLNSMINDKN ILQCHRSYLV NVKYINKIER SSDKTSYKIC FYNTTDTALL GNNYKKCIIE
RFNNAIGGDI NDRI
//
