ID U2ME69_9FIRM Unreviewed; 243 AA.
AC U2ME69;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=RUMCAL_00021 {ECO:0000313|EMBL:ERJ97583.1};
OS Ruminococcus callidus ATCC 27760.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ97583.1, ECO:0000313|Proteomes:UP000016662};
RN [1] {ECO:0000313|EMBL:ERJ97583.1, ECO:0000313|Proteomes:UP000016662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ97583.1,
RC ECO:0000313|Proteomes:UP000016662};
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 (JUL-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:ERJ97583.1}.
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DR EMBL; AWVF01000003; ERJ97583.1; -; Genomic_DNA.
DR RefSeq; WP_021682109.1; NZ_KI260403.1.
DR AlphaFoldDB; U2ME69; -.
DR STRING; 411473.RUMCAL_00021; -.
DR GeneID; 78475358; -.
DR PATRIC; fig|411473.3.peg.19; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_2_9; -.
DR OrthoDB; 1848513at2; -.
DR Proteomes; UP000016662; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR CDD; cd00156; REC; 1.
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 DNA-binding {ECO:0000313|EMBL:ERJ97583.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 3..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 135..236
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 243 AA; 28592 MW; 910FEBF8914F8050 CRC64;
MIQIAIVDDQ TEAISGILSV FQQWEKENHV YFEIDTYTDA DLFCDAIFDK KYQALFLDLD
MPKKSGFDIS QFLRELGNNT PIVYITNRDD LMQKAFQYKV LGFVRKDKIQ EELPFAISCV
VQEIQKKNSH VMIFAAHRQK KEYYNLPVSD ILYIESENHQ TKIYTVSTKD AIITRDSLRS
YMEKEEFQGF IPISVSCIVN IEHIFSIEKD TLVLDNKKVL FISRRKVKSV KEMFQQKTRR
NII
//
