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Database: UniProt
Entry: A0A0V8QDJ1_9FIRM
LinkDB: A0A0V8QDJ1_9FIRM
Original site: A0A0V8QDJ1_9FIRM 
ID   A0A0V8QDJ1_9FIRM        Unreviewed;       239 AA.
AC   A0A0V8QDJ1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=ASU35_12710 {ECO:0000313|EMBL:KSV58478.1};
OS   Acetivibrio ethanolgignens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV58478.1, ECO:0000313|Proteomes:UP000054874};
RN   [1] {ECO:0000313|EMBL:KSV58478.1, ECO:0000313|Proteomes:UP000054874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV58478.1,
RC   ECO:0000313|Proteomes:UP000054874};
RA   Zou Y., Xue W., Luo G., Lv M.;
RT   "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT   bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL   Submitted (NOV-2015) 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:KSV58478.1}.
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DR   EMBL; LNAM01000170; KSV58478.1; -; Genomic_DNA.
DR   RefSeq; WP_058353271.1; NZ_LNAM01000170.1.
DR   AlphaFoldDB; A0A0V8QDJ1; -.
DR   STRING; 290052.ASU35_12710; -.
DR   OrthoDB; 9774865at2; -.
DR   Proteomes; UP000054874; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054874}.
FT   DOMAIN          3..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          135..234
FT                   /note="HTH LytTR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50930"
FT   MOD_RES         60
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   239 AA;  28568 MW;  019BBDD63EEF79D5 CRC64;
     MVHIWICDDD KEFLEKFVMV IQEAMESLKQ EFRIRKYTDA KQLQFELEDI NKPVDIFFLD
     ILIGEENGIN LAQEIRKRKG ETPIVFLSMN KEYVFDAFDV MPLKYLLKGK FTTEEVREIL
     QKAVNLIKEN EKKMFIYKKG HFLHQLPLKE IHYFEVMNRL ITIHGDGICE EFYSTMDQVE
     KTVENSQFLR VHRSYLINMN QVNRIEDKAI FLFDGTEIPI GGKYVENIQK YFKFLLSRI
//
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