ID A0A1G6DXW7_9FIRM Unreviewed; 340 AA.
AC A0A1G6DXW7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02910298_02537 {ECO:0000313|EMBL:SDB49996.1};
OS Pseudobutyrivibrio sp. YE44.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB49996.1, ECO:0000313|Proteomes:UP000198713};
RN [1] {ECO:0000313|Proteomes:UP000198713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMXT01000011; SDB49996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6DXW7; -.
DR STRING; 1520802.SAMN02910298_02537; -.
DR OrthoDB; 9804747at2; -.
DR Proteomes; UP000198713; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR PANTHER; PTHR45228:SF4; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 4..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 142..337
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 164..286
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 340 AA; 37845 MW; B6970FE82DA50722 CRC64;
MIPQIIIVDD DPIILKGAWT TLTGAGFKVV ALKSGEALFN HMKDNPAPDL ILMDISMPEM
DGFGVIKELK KSENGWRDTP VIFLTANEDE DAETKGLSLG AMDFIRKPFV ASVLVLRVKH
AVELIRLQKD LEGMVAEKTK ENENLFMHVV ESLADAIDAK DNYTNGHSGR VADYSKEIAK
RYGYDEKKQE KIFMMGLLHD VGKIGVPDEV INKPGRLTDE EFAKIKKHPG IGGKILSNIK
EMPELAAGAK WHHERYDGKG YPQGLSGDDI PEEARIIAVA DAYDAMTSNR SYRGSLPQQI
VRGEIEKGKG SQFDPRFADI MLGMIDEDTE YSMRDNSCED
//
