ID A0A1M7CZT9_9FIRM Unreviewed; 526 AA.
AC A0A1M7CZT9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=SAMN02745136_05564 {ECO:0000313|EMBL:SHL72673.1};
OS Anaerocolumna jejuensis DSM 15929.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHL72673.1, ECO:0000313|Proteomes:UP000184386};
RN [1] {ECO:0000313|EMBL:SHL72673.1, ECO:0000313|Proteomes:UP000184386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15929 {ECO:0000313|EMBL:SHL72673.1,
RC ECO:0000313|Proteomes:UP000184386};
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; FRAC01000048; SHL72673.1; -; Genomic_DNA.
DR RefSeq; WP_073280441.1; NZ_FRAC01000048.1.
DR AlphaFoldDB; A0A1M7CZT9; -.
DR STRING; 1121322.SAMN02745136_05564; -.
DR OrthoDB; 1974963at2; -.
DR Proteomes; UP000184386; Unassembled WGS sequence.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17536; REC_YesN-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR PANTHER; PTHR43280; ARAC-FAMILY TRANSCRIPTIONAL REGULATOR; 1.
DR PANTHER; PTHR43280:SF2; BIFUNCTIONAL TRANSCRIPTIONAL ACTIVATOR_DNA REPAIR ENZYME ADAA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000184386}.
FT DOMAIN 2..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 425..523
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 526 AA; 61764 MW; 77A27B75CBC25BB1 CRC64;
MNLLIVDDQP MVVEGILAGV DWELITIDKK FTAHNIIEAK NIIQTHQIEL LLCDIEMPMG
SGLDLYEWVI EQHYTMKCIF LTAHSDFSYA QKAVHLQGFD YLLQPVTYKE IEGSLQKAID
QIKMDTTVKS YYNYALDLKK REKQTLSSLL REYLLALRSD VKEVVQYVSV LSYTLEADSS
CEILMIQLFD FEGERWENDL LFYAIDNIWN ELLTIKIGKL IVICLDSEHF ILLYQKQDER
LDLKQKMMLF MRTAEQLFRC KVALYPGKTT IFSEIPDEVK RLEKRSRKNV IKKDGILEAY
NTMEMGQEYI SPDCNKWAQY IKDGYYDLLK EEACKYLDCM TQSGRMNDEA LRKFHKDYVY
LFWEGIKNSG NVKSDLYMEG ESDYNYEALM NSYTSVIRMK SLIVFTMNYL KGMDNQENFN
ESRMDEILDY IHKNIQKNIT RKDIAEAVYL NPEYLSRLFK KEKGIKLSDY IQQEKMNIAN
HLLRTTNFSV SIVASKVGYS NFSHFAQSFK RVFGISPSEI KQENHK
//