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Database: UniProt
Entry: A0A0A7FTX1_9CLOT
LinkDB: A0A0A7FTX1_9CLOT
Original site: A0A0A7FTX1_9CLOT 
ID   A0A0A7FTX1_9CLOT        Unreviewed;       230 AA.
AC   A0A0A7FTX1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=U729_271 {ECO:0000313|EMBL:AIY83062.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83062.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY83062.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY83062.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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; CP006905; AIY83062.1; -; Genomic_DNA.
DR   RefSeq; WP_039311069.1; NZ_CP006905.1.
DR   AlphaFoldDB; A0A0A7FTX1; -.
DR   KEGG; cbv:U729_271; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OrthoDB; 9790442at2; -.
DR   Proteomes; UP000030635; 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; cd18159; REC_OmpR_NsrR-like; 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:SF31; TRANSCRIPTIONAL REGULATORY PROTEIN YXDJ; 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:UP000030635};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          4..117
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          130..228
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        130..228
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   230 AA;  27365 MW;  AE1615D2B7FB8072 CRC64;
     MNYKIYIIED DVSIGHLLKD YINKYGFDVK VISDFENVMN EFDEFNPDIV LLDVNLPKYD
     GFYWCRKIRQ KSKAPIIFIS ARDSGMDQVM ALESGGDDYI TKPFYYEVVM AKIKSHIRRA
     YGDYAHKINE RIVELDELRF YPERSELEFN NKNLIITKKE GILLEHLIKR YPKVVSRDFL
     LEKIWDDIEF VEENTLNVNV SRIRKRLREL GIENSVETVR GLGYRLNKTW
//
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