ID Q2L5V6_CLOPF Unreviewed; 224 AA. AC Q2L5V6; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 10-FEB-2021, entry version 82. DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672}; OS Clostridium perfringens. OG Plasmid pCPF4969 {ECO:0000313|EMBL:BAE79034.1}. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1502 {ECO:0000313|EMBL:BAE79034.1}; RN [1] {ECO:0000313|EMBL:BAE79034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=F4969 {ECO:0000313|EMBL:BAE79034.1}; RC PLASMID=pCPF4969 {ECO:0000313|EMBL:BAE79034.1}; RX PubMed=16452442; DOI=10.1128/JB.188.4.1585-1598.2006; RA Miyamoto K., Fisher D.J., Li J., Sayeed S., Akimoto S., McClane B.A.; RT "Complete sequencing and diversity analysis of the enterotoxin-encoding RT plasmids in Clostridium perfringens type A non-food-borne human RT gastrointestinal disease isolates."; RL J. Bacteriol. 188:1585-1598(2006). 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:ARBA00003221}. 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; AB236336; BAE79034.1; -; Genomic_DNA. DR RefSeq; YP_473407.1; NC_007772.1. DR PATRIC; fig|451756.6.peg.51; -. 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 transcription, DNA-templated; IEA:InterPro. DR CDD; cd00156; REC; 1. DR CDD; cd00383; trans_reg_C; 1. DR Gene3D; 1.10.10.10; -; 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; PTHR48111; 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; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 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 Plasmid {ECO:0000313|EMBL:BAE79034.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. FT DOMAIN 3..115 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 123..220 FT /note="OmpR/PhoB-type" FT /evidence="ECO:0000259|PROSITE:PS51755" FT DNA_BIND 123..220 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 224 AA; 25309 MW; 4969CD8CE10EEAF4 CRC64; MSKLLVIDDD IDMLDLVRAT LEKDGHQVDT EVDATTIQPS KCQQYDLLLL DVMMPSENGF SLCSRIRSEV DCPILFLTAK AEDTALVQGF GLGADDYIKK PFSIAELRAR VNAHLRREVR QPTHTLSRSG VRFNMQEKMA IVGEDTIFFT KGEYAISEHL ALHIGQVFTK EQLYEAVFGF DADGDSSAIV EHIKNIRAKL KAYNLNPIET VWGVGYKWRK DKIL //