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Database: UniProt
Entry: M1MSP1_9CLOT
LinkDB: M1MSP1_9CLOT
Original site: M1MSP1_9CLOT 
ID   M1MSP1_9CLOT            Unreviewed;       231 AA.
AC   M1MSP1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   Name=ycbL {ECO:0000313|EMBL:AGF54597.1};
GN   ORFNames=Cspa_c08200 {ECO:0000313|EMBL:AGF54597.1};
OS   Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF54597.1, ECO:0000313|Proteomes:UP000011728};
RN   [1] {ECO:0000313|EMBL:AGF54597.1, ECO:0000313|Proteomes:UP000011728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL   Submitted (FEB-2013) 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}.
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DR   EMBL; CP004121; AGF54597.1; -; Genomic_DNA.
DR   RefSeq; WP_015390923.1; NZ_AOIF01000144.1.
DR   AlphaFoldDB; M1MSP1; -.
DR   STRING; 36745.CLSAP_08600; -.
DR   KEGG; csr:Cspa_c08200; -.
DR   PATRIC; fig|931276.5.peg.776; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OrthoDB; 9803564at2; -.
DR   Proteomes; UP000011728; 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:SF40; SENSORY TRANSDUCTION PROTEIN REGX3; 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:UP000011728};
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          126..226
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        126..226
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   231 AA;  26287 MW;  78D90144B8241D8A CRC64;
     MKHIFFVEDN LSLINGLSFA IKKQGYEIDV ARTILEAEAL LVNKKYDLVI LDVSLPDGCG
     YDLCKKIRKT SKVPIIFLTA ADEETDIIMG LDIGGDDYIT KPFKLAVFMS KINALLRRSD
     NFIQADTELN SNGINVQLLK GEVYKNGEQL DLTTSEYKVL CLFMENPHIV LSPEQILSKL
     WDCNENYIDN NTITVYIRRL RTKIEDNPSE PQKIVTVRRM GYKWNTVDGG V
//
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