SP0F_BACSU
ID SP0F_BACSU Reviewed; 124 AA.
AC P06628;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sporulation initiation phosphotransferase F;
DE EC=2.7.-.-;
DE AltName: Full=Stage 0 sporulation protein F;
GN Name=spo0F; OrderedLocusNames=BSU37130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3003689; DOI=10.1093/nar/14.2.1063;
RA Yoshikawa H., Kazami J., Yamashita S., Chibazakura T., Sone H.,
RA Kawamura F., Oda M., Isaka M., Kobayashi Y., Saito H.;
RT "Revised assignment for the Bacillus subtilis spo0F gene and its homology
RT with spo0A and with two Escherichia coli genes.";
RL Nucleic Acids Res. 14:1063-1072(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=2997779; DOI=10.1073/pnas.82.21.7260;
RA Trach K.A., Chapman J.W., Piggot P.J., Hoch J.A.;
RT "Deduced product of the stage 0 sporulation gene spo0F shares homology with
RT the Spo0A, OmpR, and SfrA proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7260-7264(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=2457578; DOI=10.1128/jb.170.9.4194-4208.1988;
RA Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.;
RT "Complete sequence and transcriptional analysis of the spo0F region of the
RT Bacillus subtilis chromosome.";
RL J. Bacteriol. 170:4194-4208(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8528078; DOI=10.1002/pro.5560040915;
RA Feher V.A., Zapf J.W., Hoch J.A., Dahlquist F.W., Whiteley J.M.,
RA Cavanagh J.;
RT "1H, 15N, and 13C backbone chemical shift assignments, secondary structure,
RT and magnesium-binding characteristics of the Bacillus subtilis response
RT regulator, Spo0F, determined by heteronuclear high-resolution NMR.";
RL Protein Sci. 4:1801-1814(1995).
RN [7]
RP STRUCTURE BY NMR, AND PHOSPHORYLATION AT ASP-54.
RX PubMed=9254596; DOI=10.1021/bi970816l;
RA Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntosh L.P., Rance M.,
RA Skelton N.J., Dahlquist F.W., Cavanagh J.;
RT "High-resolution NMR structure and backbone dynamics of the Bacillus
RT subtilis response regulator, Spo0F: implications for phosphorylation and
RT molecular recognition.";
RL Biochemistry 36:10015-10025(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-13.
RX PubMed=8805550; DOI=10.1016/s0969-2126(96)00074-3;
RA Madhusudan X., Zapf J., Whiteley J.M., Hoch J.A., Xuong N.H.,
RA Varughese K.I.;
RT "Crystal structure of a phosphatase-resistant mutant of sporulation
RT response regulator Spo0F from Bacillus subtilis.";
RL Structure 4:679-690(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=9335530; DOI=10.1021/bi971276v;
RA Madhusudan X., Zapf J., Hoch J.A., Whiteley J.M., Xuong N.H.,
RA Varughese K.I.;
RT "A response regulatory protein with the site of phosphorylation blocked by
RT an arginine interaction: crystal structure of Spo0F from Bacillus
RT subtilis.";
RL Biochemistry 36:12739-12745(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=10997904; DOI=10.1016/s0969-2126(00)00174-x;
RA Zapf J., Sen U., Madhusudan X., Hoch J.A., Varughese K.I.;
RT "A transient interaction between two phosphorelay proteins trapped in a
RT crystal lattice reveals the mechanism of molecular recognition and
RT phosphotransfer in signal transduction.";
RL Structure 8:851-862(2000).
CC -!- FUNCTION: Key element in the phosphorelay regulating sporulation
CC initiation. Phosphorylation of spo0B during sporulation initiation.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- INTERACTION:
CC P06628; P16497: kinA; NbExp=3; IntAct=EBI-6418009, EBI-6405707;
CC P06628; Q59HN8: rapH; NbExp=2; IntAct=EBI-6418009, EBI-15913371;
CC P06628; O34327: rapJ; NbExp=2; IntAct=EBI-6418009, EBI-5246213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by KinA and KinB. Dephosphorylated by RapA and
CC RapB. {ECO:0000269|PubMed:9254596}.
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DR EMBL; X03497; CAA27217.1; -; Genomic_DNA.
DR EMBL; M11081; AAA22787.1; -; Genomic_DNA.
DR EMBL; M22039; AAA16802.1; -; Unassigned_DNA.
DR EMBL; Z49782; CAA89872.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15730.1; -; Genomic_DNA.
DR PIR; A24737; SZBS0F.
DR RefSeq; NP_391594.1; NC_000964.3.
DR RefSeq; WP_003227621.1; NZ_JNCM01000034.1.
DR PDB; 1F51; X-ray; 3.00 A; E/F/G/H=3-121.
DR PDB; 1FSP; NMR; -; A=1-124.
DR PDB; 1NAT; X-ray; 2.45 A; A=1-124.
DR PDB; 1PEY; X-ray; 2.25 A; A/B/C=1-124.
DR PDB; 1PUX; NMR; -; A=1-124.
DR PDB; 1SRR; X-ray; 1.90 A; A/B/C=1-124.
DR PDB; 2FSP; NMR; -; A=1-124.
DR PDB; 2FTK; X-ray; 3.05 A; E/F/G/H=1-124.
DR PDB; 2JVI; NMR; -; A=1-124.
DR PDB; 2JVJ; NMR; -; A=1-124.
DR PDB; 2JVK; NMR; -; A=1-124.
DR PDB; 3Q15; X-ray; 2.19 A; C/D=1-124.
DR PDBsum; 1F51; -.
DR PDBsum; 1FSP; -.
DR PDBsum; 1NAT; -.
DR PDBsum; 1PEY; -.
DR PDBsum; 1PUX; -.
DR PDBsum; 1SRR; -.
DR PDBsum; 2FSP; -.
DR PDBsum; 2FTK; -.
DR PDBsum; 2JVI; -.
DR PDBsum; 2JVJ; -.
DR PDBsum; 2JVK; -.
DR PDBsum; 3Q15; -.
DR AlphaFoldDB; P06628; -.
DR BMRB; P06628; -.
DR SMR; P06628; -.
DR DIP; DIP-58965N; -.
DR IntAct; P06628; 6.
DR STRING; 224308.BSU37130; -.
DR BindingDB; P06628; -.
DR ChEMBL; CHEMBL2111331; -.
DR PaxDb; P06628; -.
DR PRIDE; P06628; -.
DR EnsemblBacteria; CAB15730; CAB15730; BSU_37130.
DR GeneID; 50135711; -.
DR GeneID; 64305489; -.
DR GeneID; 937041; -.
DR KEGG; bsu:BSU37130; -.
DR PATRIC; fig|224308.43.peg.3893; -.
DR eggNOG; COG2204; Bacteria.
DR InParanoid; P06628; -.
DR OMA; MHFTKPF; -.
DR PhylomeDB; P06628; -.
DR BioCyc; BSUB:BSU37130-MON; -.
DR EvolutionaryTrace; P06628; -.
DR PRO; PR:P06628; -.
DR Proteomes; UP000001570; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome; Sporulation; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..124
FT /note="Sporulation initiation phosphotransferase F"
FT /id="PRO_0000081244"
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:9254596"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1SRR"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1SRR"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1SRR"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1NAT"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1SRR"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1SRR"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1SRR"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2JVJ"
SQ SEQUENCE 124 AA; 14228 MW; 4130377E3558D698 CRC64;
MMNEKILIVD DQYGIRILLN EVFNKEGYQT FQAANGLQAL DIVTKERPDL VLLDMKIPGM
DGIEILKRMK VIDENIRVII MTAYGELDMI QESKELGALT HFAKPFDIDE IRDAVKKYLP
LKSN
