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Database: UniProt
Entry: A0A1M6E1I6_9FIRM
LinkDB: A0A1M6E1I6_9FIRM
Original site: A0A1M6E1I6_9FIRM 
ID   A0A1M6E1I6_9FIRM        Unreviewed;       233 AA.
AC   A0A1M6E1I6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN02745691_00830 {ECO:0000313|EMBL:SHI79367.1};
OS   Parasporobacterium paucivorans DSM 15970.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Parasporobacterium.
OX   NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHI79367.1, ECO:0000313|Proteomes:UP000184342};
RN   [1] {ECO:0000313|EMBL:SHI79367.1, ECO:0000313|Proteomes:UP000184342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15970 {ECO:0000313|EMBL:SHI79367.1,
RC   ECO:0000313|Proteomes:UP000184342};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQYT01000007; SHI79367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6E1I6; -.
DR   STRING; 1122934.SAMN02745691_00830; -.
DR   OrthoDB; 9790442at2; -.
DR   Proteomes; UP000184342; Unassembled WGS sequence.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111:SF73; ALKALINE PHOSPHATASE SYNTHESIS TRANSCRIPTIONAL REGULATORY PROTEIN PHOP; 1.
DR   PANTHER; PTHR48111; REGULATOR OF RPOS; 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; SSF52172; CheY-like; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
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:UP000184342};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          5..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          129..230
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        129..230
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   233 AA;  26374 MW;  88A2517FA527DF60 CRC64;
     MSVKEILVVD DEPKILEVVS SYLESKGFKV FTAETGGEAL DIFAKNRISL VVLDLMLPDI
     SGEEICTRLR KESRVPVIML TAKTQENDLL NGLQSGADDY ITKPFSLKEL HARIEAILRR
     SAEDLAPLLA KLTWNEGDLI IDFDRNVVKK GGEEVSLTPI EWRIISALVK YPKKVFTRDE
     LIDIAFDAGF DGYDRVIDTH IKNLRQKIED DTKNTIYILT VRGRGYKFGG ERQ
//
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