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Database: UniProt
Entry: F6DKF9_DESRL
LinkDB: F6DKF9_DESRL
Original site: F6DKF9_DESRL 
ID   F6DKF9_DESRL            Unreviewed;       222 AA.
AC   F6DKF9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   OrderedLocusNames=Desru_0943 {ECO:0000313|EMBL:AEG59219.1};
OS   Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS   (Desulfotomaculum ruminis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG59219.1, ECO:0000313|Proteomes:UP000009234};
RN   [1] {ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA   Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA   Spring S., Klenk H.-P., Woyke T.;
RT   "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG59219.1, ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RX   PubMed=23408247; DOI=10.4056/sigs.3226659;
RA   Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA   Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA   Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA   Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA   Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT   "Complete genome sequence of the sulfate-reducing firmicute
RT   Desulfotomaculum ruminis type strain (DL(T)).";
RL   Stand. Genomic Sci. 7:304-319(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; CP002780; AEG59219.1; -; Genomic_DNA.
DR   RefSeq; WP_013840990.1; NC_015589.1.
DR   AlphaFoldDB; F6DKF9; -.
DR   STRING; 696281.Desru_0943; -.
DR   KEGG; dru:Desru_0943; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OMA; EMGSDDY; -.
DR   OrthoDB; 9790454at2; -.
DR   Proteomes; UP000009234; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17574; REC_OmpR; 1.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.690; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR   PANTHER; PTHR48111:SF24; TRANSCRIPTIONAL REGULATORY PROTEIN CSSR; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01091}; Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009234};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          127..221
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        127..221
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         51
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   222 AA;  25999 MW;  145876BE13EBF756 CRC64;
     MFRIYLVEDE KNLNQILTSY LEKEGWEIRS FTEGEPALQA VKERPNLWIL DIMLPDIDGY
     QVLRKIKEDT PEVPVIFISA RDADIDRIIG LEMGSDDYLA KPFLPRELVI RTHRLLERVY
     TSTEPVKPVI NLHPYLLDDG KREIRQGSNI IELTTKEYDL ALLFAKHKGQ ALSRDQIINF
     VWGENYVGTD RSVDDLIRRI RKKLPHLRIE TIYGFGYRMI AQ
//
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