ID C7GGV2_9FIRM Unreviewed; 236 AA.
AC C7GGV2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=ROSINTL182_09174 {ECO:0000313|EMBL:EEU98969.1};
OS Roseburia intestinalis L1-82.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=536231 {ECO:0000313|EMBL:EEU98969.1, ECO:0000313|Proteomes:UP000004828};
RN [1] {ECO:0000313|EMBL:EEU98969.1, ECO:0000313|Proteomes:UP000004828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L1-82 {ECO:0000313|EMBL:EEU98969.1,
RC ECO:0000313|Proteomes:UP000004828};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2009) 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:EEU98969.1}.
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DR EMBL; ABYJ02000255; EEU98969.1; -; Genomic_DNA.
DR RefSeq; WP_006859240.1; NZ_LR027880.1.
DR AlphaFoldDB; C7GGV2; -.
DR GeneID; 61433280; -.
DR HOGENOM; CLU_000445_14_2_9; -.
DR Proteomes; UP000004828; 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 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:EEU98969.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 3..121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 135..233
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 236 AA; 27658 MW; 79007B11BE187EC0 CRC64;
MIRIAICDDE KNIRTYLSSL VRKQNIECEI TEYASTDEYL SDQKEHDLLF LDIEMKSVAS
GMDGMSMAKQ IRATELTKQP IIIFVTGYEK YVYDAFDVGA FQYLLKPIDE QRFAQVFRRA
AEQIISEAEQ QKKTLVIQYA NTSKAIPLDH IYYLESQSHK VVIHMKEEEL EYYAKLGDLE
EELQGQFFRI HKGYLVNLAC IDEYNKTEVT LVNGDKLLIS KYKYPDFVKA YLRYMQ
//
