ID J4UC83_9FIRM Unreviewed; 235 AA.
AC J4UC83;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=HMPREF1140_0867 {ECO:0000313|EMBL:EJP20382.1};
OS Lachnoanaerobaculum sp. ICM7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP20382.1, ECO:0000313|Proteomes:UP000006599};
RN [1] {ECO:0000313|EMBL:EJP20382.1, ECO:0000313|Proteomes:UP000006599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP20382.1,
RC ECO:0000313|Proteomes:UP000006599};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJP20382.1}.
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DR EMBL; ALJL01000023; EJP20382.1; -; Genomic_DNA.
DR RefSeq; WP_007595143.1; NZ_ALJL01000023.1.
DR AlphaFoldDB; J4UC83; -.
DR PATRIC; fig|936594.3.peg.1647; -.
DR Proteomes; UP000006599; 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; cd00383; trans_reg_C; 1.
DR Gene3D; 3.40.50.2300; -; 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:SF85; RESPONSE REGULATOR SAER; 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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 6..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 136..233
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DNA_BIND 136..233
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 235 AA; 27065 MW; E5954D5DF9A033B2 CRC64;
MAEKQRILIV DDDENIAELI SLYLMKECYE TKIVGDGESA LSDFDEFKPH LVLLDLMLPG
IDGYQVCREI RAKSGTPIIM LSAKGEVFDK VLGLELGADD YMIKPFDSKE LIARVKAVIR
RYNNSTISLP EVHTGGEYVE YPDLNVNMTN YAVTYLGKNV EMPPKELELL YFLSSHPNQV
FTREQLLDNI WGYEYIGDTR TVDVHIKRLR EKIHDNKFWS ISTVWGIGYK FEVKK
//
