ID   SP0F_BACTK              Reviewed;         122 AA.
AC   P52942;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Sporulation initiation phosphotransferase F;
DE            EC=2.7.-.-;
DE   AltName: Full=Stage 0 sporulation protein F;
GN   Name=spo0F;
OS   Bacillus thuringiensis subsp. kurstaki.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=29339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EG10368;
RX   PubMed=7514590; DOI=10.1128/jb.176.10.2835-2845.1994;
RA   Baum J.A.;
RT   "Tn5401, a new class II transposable element from Bacillus thuringiensis.";
RL   J. Bacteriol. 176:2835-2845(1994).
CC   -!- FUNCTION: Key element in the phosphorelay regulating sporulation
CC       initiation. Phosphorylation of spo0B during sporulation initiation (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by KinA and KinB. {ECO:0000250}.
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DR   EMBL; U03553; AAA64587.1; -; Genomic_DNA.
DR   PIR; I40583; I40583.
DR   AlphaFoldDB; P52942; -.
DR   SMR; P52942; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein; Sporulation;
KW   Transferase; Two-component regulatory system.
FT   CHAIN           1..122
FT                   /note="Sporulation initiation phosphotransferase F"
FT                   /id="PRO_0000081245"
FT   DOMAIN          4..118
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   122 AA;  13759 MW;  E614D7D9584419EE CRC64;
     MEGKILIVDD QYGIRVLLHE VFQKEGYQTF QAANGFQALD IVKKDNPDLV VLDMKIPGMD
     GIEIFKACKE IDESIKVILM SAYGELDMIQ EAKDLGALMH FAKPFDIDEI RQAVRNELAV
     EA