ID B8FR15_DESHD Unreviewed; 251 AA.
AC B8FR15;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN OrderedLocusNames=Dhaf_3686 {ECO:0000313|EMBL:ACL21702.1};
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL21702.1, ECO:0000313|Proteomes:UP000007726};
RN [1] {ECO:0000313|EMBL:ACL21702.1, ECO:0000313|Proteomes:UP000007726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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}.
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DR EMBL; CP001336; ACL21702.1; -; Genomic_DNA.
DR RefSeq; WP_015944723.1; NC_011830.1.
DR AlphaFoldDB; B8FR15; -.
DR KEGG; dhd:Dhaf_3686; -.
DR HOGENOM; CLU_000445_14_1_9; -.
DR Proteomes; UP000007726; Chromosome.
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}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 145..250
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000259|PROSITE:PS50930"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 251 AA; 28621 MW; A93907111D8E8297 CRC64;
MVLRVLIVED DANMRLILKR ALFGIPNVEV VGEAGNGTEA VGLAAELEPH VIIMDVDLPG
KDGVEASREI LNISPDVFLV YATGHPEYMA EAFEMYAFDY LVKPYRMERL TQTITRIQKL
IESKGKGIQQ SREEGSNSVG IKNKIAVKIE GKLTLIDTTK IIYTTRDKRK TVIHTIDGKV
TVNESLEGLE KRLAGYNFMR THRSYLVNLD RIVEIQPLSR NEYLVIFGET KERAYITDEK
YRELQIKLNF R
//
