SP0B_BACSU
ID SP0B_BACSU Reviewed; 192 AA.
AC P06535;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sporulation initiation phosphotransferase B;
DE EC=2.7.-.-;
DE AltName: Full=Stage 0 sporulation protein B;
DE AltName: Full=Stage 0 sporulation protein D;
GN Name=spo0B; Synonyms=spo0D; OrderedLocusNames=BSU27930;
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=3918016; DOI=10.1128/jb.161.2.556-562.1985;
RA Ferrari F.A., Trach K.A., Hoch J.A.;
RT "Sequence analysis of the spo0B locus reveals a polycistronic transcription
RT unit.";
RL J. Bacteriol. 161:556-562(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2537815; DOI=10.1128/jb.171.3.1362-1371.1989;
RA Trach K., Hoch J.A.;
RT "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an
RT essential GTP-binding protein.";
RL J. Bacteriol. 171:1362-1371(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6438629; DOI=10.1073/pnas.81.22.7012;
RA Bouvier J., Stragier P., Bonamy C., Szulmajster J.;
RT "Nucleotide sequence of the spo0B gene of Bacillus subtilis and regulation
RT of its expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7012-7016(1984).
RN [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9809070; DOI=10.1016/s1097-2765(00)80148-3;
RA Varughese K.I., Madhusudan X., Zhou X.Z., Whiteley J.M., Hoch J.A.;
RT "Formation of a novel four-helix bundle and molecular recognition sites by
RT dimerization of a response regulator phosphotransferase.";
RL Mol. Cell 2:485-493(1998).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION AT HIS-30, AND MUTAGENESIS OF HIS-30.
RX PubMed=9726997; DOI=10.1074/jbc.273.37.23849;
RA Tzeng Y.L., Zhou X.Z., Hoch J.A.;
RT "Phosphorylation of the Spo0B response regulator phosphotransferase of the
RT phosphorelay initiating development in Bacillus subtilis.";
RL J. Biol. Chem. 273:23849-23855(1998).
CC -!- FUNCTION: Key element in the phosphorelay regulating sporulation
CC initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from
CC spo0F to spo0A.
CC -!- SUBUNIT: Homodimer. Dimerization is essential for activity as both
CC monomers contribute to the formation of the active site.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed during sporulation.
CC -!- PTM: Phosphorylated by spo0F. {ECO:0000269|PubMed:9726997}.
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DR EMBL; X02655; CAA26489.1; -; Genomic_DNA.
DR EMBL; M24537; AAA22504.1; -; Genomic_DNA.
DR EMBL; K02664; AAB05348.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14753.1; -; Genomic_DNA.
DR PIR; A22974; SZBS0B.
DR RefSeq; NP_390671.1; NC_000964.3.
DR RefSeq; WP_004399131.1; NZ_JNCM01000036.1.
DR PDB; 1F51; X-ray; 3.00 A; A/B/C/D=11-192.
DR PDB; 1IXM; X-ray; 2.60 A; A/B=1-192.
DR PDB; 2FTK; X-ray; 3.05 A; A/B/C/D=1-192.
DR PDBsum; 1F51; -.
DR PDBsum; 1IXM; -.
DR PDBsum; 2FTK; -.
DR AlphaFoldDB; P06535; -.
DR SMR; P06535; -.
DR STRING; 224308.BSU27930; -.
DR iPTMnet; P06535; -.
DR PaxDb; P06535; -.
DR PRIDE; P06535; -.
DR EnsemblBacteria; CAB14753; CAB14753; BSU_27930.
DR GeneID; 935956; -.
DR KEGG; bsu:BSU27930; -.
DR PATRIC; fig|224308.179.peg.3034; -.
DR eggNOG; COG3290; Bacteria.
DR OMA; RHARHDW; -.
DR BioCyc; BSUB:BSU27930-MON; -.
DR EvolutionaryTrace; P06535; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.30; -; 1.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR037100; Spo0B_C_sf.
DR InterPro; IPR039506; SPOB_a.
DR InterPro; IPR016122; SpoOB_C.
DR Pfam; PF14689; SPOB_a; 1.
DR Pfam; PF14682; SPOB_ab; 1.
DR SMART; SM01317; SPOB_ab; 1.
DR SUPFAM; SSF55890; SSF55890; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Phosphoprotein; Reference proteome;
KW Sensory transduction; Sporulation; Transferase.
FT CHAIN 1..192
FT /note="Sporulation initiation phosphotransferase B"
FT /id="PRO_0000072052"
FT MOD_RES 30
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:9726997"
FT MUTAGEN 30
FT /note="H->A: Loss of sporulation."
FT /evidence="ECO:0000269|PubMed:9726997"
FT HELIX 15..44
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 48..69
FT /evidence="ECO:0007829|PDB:1IXM"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1IXM"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:1IXM"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:1IXM"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1F51"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1IXM"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1IXM"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1F51"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1IXM"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:1IXM"
SQ SEQUENCE 192 AA; 22543 MW; 3A9A38B5FFB55647 CRC64;
MKDVSKNQEE NISDTALTNE LIHLLGHSRH DWMNKLQLIK GNLSLQKYDR VFEMIEEMVI
DAKHESKLSN LKTPHLAFDF LTFNWKTHYM TLEYEVLGEI KDLSAYDQKL AKLMRKLFHL
FDQAVSRESE NHLTVSLQTD HPDRQLILYL DFHGAFADPS AFDDIRQNGY EDVDIMRFEI
TSHECLIEIG LD
