BOFA_BACSU
ID BOFA_BACSU Reviewed; 87 AA.
AC P24282;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Sigma-K factor-processing regulatory protein BofA;
DE AltName: Full=Bypass-of-forespore protein A;
GN Name=bofA; OrderedLocusNames=BSU00230;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / YB886 / BG214;
RX PubMed=2124672; DOI=10.1093/nar/18.23.6771;
RA Alonso J.C., Shirahige K., Ogasawara N.;
RT "Molecular cloning, genetic characterization and DNA sequence analysis of
RT the recM region of Bacillus subtilis.";
RL Nucleic Acids Res. 18:6771-6777(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 55.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP CHARACTERIZATION.
RX PubMed=1577688; DOI=10.1128/jb.174.10.3177-3184.1992;
RA Ricca E., Cutting S.M., Losick R.;
RT "Characterization of bofA, a gene involved in intercompartmental regulation
RT of pro-sigma K processing during sporulation in Bacillus subtilis.";
RL J. Bacteriol. 174:3177-3184(1992).
RN [6]
RP TOPOLOGY.
RX PubMed=9141672; DOI=10.1099/00221287-143-4-1053;
RA Varcamonti M., Marasco R., de Felice M., Sacco M.;
RT "Membrane topology analysis of the Bacillus subtilis BofA protein involved
RT in pro-sigma K processing.";
RL Microbiology 143:1053-1058(1997).
RN [7]
RP FUNCTION IN STABILIZING SPOIVFA.
RX PubMed=10464210; DOI=10.1128/jb.181.17.5384-5388.1999;
RA Resnekov O.;
RT "Role of the sporulation protein BofA in regulating activation of the
RT Bacillus subtilis developmental transcription factor sigmaK.";
RL J. Bacteriol. 181:5384-5388(1999).
RN [8]
RP SUBUNIT, AND FUNCTION.
RX PubMed=11959848; DOI=10.1101/gad.977702;
RA Rudner D.Z., Losick R.;
RT "A sporulation membrane protein tethers the pro-sigmaK processing enzyme to
RT its inhibitor and dictates its subcellular localization.";
RL Genes Dev. 16:1007-1018(2002).
RN [9]
RP FUNCTION.
RX PubMed=15087499; DOI=10.1073/pnas.0307709101;
RA Zhou R., Kroos L.;
RT "BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an
RT intercompartmental signaling pathway during Bacillus subtilis
RT sporulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6385-6390(2004).
CC -!- FUNCTION: Involved in the mediation of the intercompartmental coupling
CC of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB-
CC processing activity until a signal has been received from the
CC forespore. Could inhibit SpoIVFB metalloprotease activity by
CC coordinating a zinc in the SpoIVFB active site, preventing access of a
CC water molecule and the sequence of pro-sigma K, which are necessary for
CC peptide bond hydrolysis to produce sigma-K.
CC {ECO:0000269|PubMed:10464210, ECO:0000269|PubMed:11959848,
CC ECO:0000269|PubMed:15087499}.
CC -!- SUBUNIT: Forms a complex with SpoIVFA and SpoIVFB localized in the
CC mother cell membrane surrounding the forespore.
CC {ECO:0000269|PubMed:11959848}.
CC -!- SUBCELLULAR LOCATION: Forespore outer membrane; Multi-pass membrane
CC protein.
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DR EMBL; X17014; CAA34880.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05259.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11799.2; -; Genomic_DNA.
DR PIR; B41869; B41869.
DR RefSeq; NP_387904.2; NC_000964.3.
DR RefSeq; WP_003225421.1; NZ_JNCM01000024.1.
DR AlphaFoldDB; P24282; -.
DR SMR; P24282; -.
DR STRING; 224308.BSU00230; -.
DR PaxDb; P24282; -.
DR EnsemblBacteria; CAB11799; CAB11799; BSU_00230.
DR GeneID; 64301839; -.
DR GeneID; 937025; -.
DR KEGG; bsu:BSU00230; -.
DR PATRIC; fig|224308.179.peg.23; -.
DR eggNOG; ENOG50333K6; Bacteria.
DR OMA; FINMAGK; -.
DR BioCyc; BSUB:BSU00230-MON; -.
DR PRO; PR:P24282; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR010001; BofA.
DR Pfam; PF07441; BofA; 1.
DR TIGRFAMs; TIGR02862; spore_BofA; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..87
FT /note="Sigma-K factor-processing regulatory protein BofA"
FT /id="PRO_0000064969"
FT TOPO_DOM 1..2
FT /note="Forespore intermembrane space"
FT /evidence="ECO:0000305|PubMed:9141672"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 24..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9141672"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 58..87
FT /note="Forespore intermembrane space"
FT /evidence="ECO:0000305|PubMed:9141672"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with SpoIVFB"
FT CONFLICT 55
FT /note="G -> C (in Ref. 1; CAA34880 and 2; BAA05259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 8964 MW; F9B1CB8E6826B70E CRC64;
MEPIFIIGII LGLVILLFLS GSAAKPLKWI GITAVKFVAG ALLLVCVNMF GGSLGIHVPI
NLVTTAISGI LGIPGIAALV VIKQFII
