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Database: UniProt
Entry: A0A1T4YEL1_9CLOT
LinkDB: A0A1T4YEL1_9CLOT
Original site: A0A1T4YEL1_9CLOT 
ID   A0A1T4YEL1_9CLOT        Unreviewed;       227 AA.
AC   A0A1T4YEL1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN   ORFNames=SAMN05443428_14119 {ECO:0000313|EMBL:SKB00130.1};
OS   Caloramator quimbayensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Caloramator.
OX   NCBI_TaxID=1147123 {ECO:0000313|EMBL:SKB00130.1, ECO:0000313|Proteomes:UP000190105};
RN   [1] {ECO:0000313|EMBL:SKB00130.1, ECO:0000313|Proteomes:UP000190105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 833 {ECO:0000313|EMBL:SKB00130.1,
RC   ECO:0000313|Proteomes:UP000190105};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUYH01000041; SKB00130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4YEL1; -.
DR   STRING; 1147123.SAMN05443428_14119; -.
DR   OrthoDB; 9790442at2; -.
DR   Proteomes; UP000190105; 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; 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   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          128..227
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51755"
FT   DNA_BIND        128..227
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   227 AA;  26387 MW;  CA6FDCFE07195CD7 CRC64;
     MEYRILIIDD EENLVKGIKY NLELDGYEVD VAYDGEEALM KMDENIYNLI VLDIMLPKID
     GLVLLKKIRE RSSIPIIMLT AKGEDEDKVL GFEYGADDYM TKPFNILELR ARIKALLRRT
     YDIVTNKADI IREGDIMIDV PSRKVNISGK PVDLTSKEFD ILFLLLTNPG KIYSRETLLE
     IIWGYDYYGD SRTVDVHIRR LREKIEKDPG NPQYVLTKWG VGYYYKG
//
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