ID A0A0C1U2M2_9CLOT Unreviewed; 190 AA.
AC A0A0C1U2M2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=U732_1324 {ECO:0000313|EMBL:KIE47104.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47104.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE47104.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47104.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE47104.1}.
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DR EMBL; AYSO01000015; KIE47104.1; -; Genomic_DNA.
DR RefSeq; WP_039632234.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1U2M2; -.
DR STRING; 29341.RSJ17_13610; -.
DR OrthoDB; 9779069at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
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; IPR005561; ANTAR.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008327; Sig_transdc_resp-reg_antiterm.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43367; -; 1.
DR PANTHER; PTHR43367:SF1; TWO-COMPONENT RESPONSE REGULATOR-LIKE APRR6-RELATED; 1.
DR Pfam; PF03861; ANTAR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF036382; RR_antiterm; 1.
DR SMART; SM01012; ANTAR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50921; ANTAR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT DOMAIN 4..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 125..186
FT /note="ANTAR"
FT /evidence="ECO:0000259|PROSITE:PS50921"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 190 AA; 21432 MW; 3801B58F7D453EDB CRC64;
MTKRIVIADD EPITRMDIRE MLEEAGYSVV AEASDGFDAI EMCRKHLPDL IIMDIKMPLL
DGLNASKIIN QEGLASGIVL LSAYSDKTFI EKAKEVGVIG YLVKPLDNKS LIPNIEVCLS
KSREFKKIKD DIKSVEKKLQ ARKIIEKAKG ILMRQNGITE DEAYSNIRNL SMKKRVTMEE
ISQIIVMSEE
//
