ID R5PUY2_9FIRM Unreviewed; 265 AA.
AC R5PUY2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672, ECO:0000256|PIRNR:PIRNR002937};
GN ORFNames=BN766_01006 {ECO:0000313|EMBL:CCZ19993.1};
OS Candidatus Apopatosoma intestinale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Apopatosoma.
OX NCBI_TaxID=1262966 {ECO:0000313|EMBL:CCZ19993.1, ECO:0000313|Proteomes:UP000018243};
RN [1] {ECO:0000313|EMBL:CCZ19993.1, ECO:0000313|Proteomes:UP000018243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:724 {ECO:0000313|Proteomes:UP000018243};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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, ECO:0000256|PIRNR:PIRNR002937}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR002937,
CC ECO:0000256|PIRSR:PIRSR002937-1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR002937}.
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:CCZ19993.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAZP010000050; CCZ19993.1; -; Genomic_DNA.
DR AlphaFoldDB; R5PUY2; -.
DR STRING; 1262966.BN766_01006; -.
DR Proteomes; UP000018243; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0051606; P:detection of stimulus; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
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; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014879; Spo0A_C.
DR InterPro; IPR012052; Spore_0_A.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR02875; spore_0_A; 1.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF1; TWO-COMPONENT RESPONSE REGULATOR ORR33; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF08769; Spo0A_C; 1.
DR PIRSF; PIRSF002937; Res_reg_Spo0A; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|PIRNR:PIRNR002937};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002937};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002937};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR002937};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002937,
KW ECO:0000256|PIRSR:PIRSR002937-1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000018243};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR002937};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|PIRNR:PIRNR002937};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR002937};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR002937};
KW Two-component regulatory system {ECO:0000256|PIRNR:PIRNR002937}.
FT DOMAIN 6..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002937-1"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 265 AA; 30248 MW; 7294C731365E4E8C CRC64;
MEQKVRILIA DENVEFRMNL RENLTRAGME IVEEASDGTD ILTKIKRTTP DIVFIDIWLP
KGDPIQIIKK SKLLFPNPLQ APDFIALSYC SNPNLFLEAS EAGATFCIQK PVEYATLFDR
IMRIYRNRQN NFRIPLSSMR TGSGSDEDAD LETQVTKILH KIGVPAHIKG YQYLRTAIIM
TVENNNLINS VTKILYPSVA KTYETTSSRV ERAIRHAIEV AWDRGDLDVL NSYFGYTIQN
ERGKPTNSEF IAMISDNLRL KNRIS
//
