SP4FB_BACSU
ID SP4FB_BACSU Reviewed; 288 AA.
AC P26937;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Stage IV sporulation protein FB;
DE EC=3.4.24.-;
GN Name=spoIVFB; Synonyms=bofB; OrderedLocusNames=BSU27970;
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;
RX PubMed=1942049; DOI=10.1016/0022-2836(91)90931-u;
RA Cutting S.M., Roels S., Losick R.;
RT "Sporulation operon spoIVF and the characterization of mutations that
RT uncouple mother-cell from forespore gene expression in Bacillus subtilis.";
RL J. Mol. Biol. 221:1237-1256(1991).
RN [2]
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 [3]
RP MUTAGENESIS OF HIS-43; GLU-44 AND HIS-47.
RX PubMed=10809718; DOI=10.1128/jb.182.11.3305-3309.2000;
RA Yu Y.-T., Kroos L.;
RT "Evidence that SpoIVFB is a novel type of membrane metalloprotease
RT governing intercompartmental communication during Bacillus subtilis
RT sporulation.";
RL J. Bacteriol. 182:3305-3309(2000).
RN [4]
RP SUBUNIT.
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 [5]
RP INHIBITION BY BOFA.
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: Implicated in the coupling of mother cell to forespore gene
CC expression. Required for spore formation. Processes the pro-sigma K
CC factor.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Forms a complex with SpoIVFA and BofA localized in the mother-
CC cell membrane surrounding the forespore. {ECO:0000269|PubMed:11959848}.
CC -!- INTERACTION:
CC P26937; P12254: sigK; NbExp=2; IntAct=EBI-15806037, EBI-15806052;
CC -!- SUBCELLULAR LOCATION: Forespore outer membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Transcribed during the stage II, but not required
CC until stage IV of sporulation.
CC -!- MISCELLANEOUS: Could be held inactive when BofA provides a fourth zinc
CC ligand, preventing access to a water molecule and the sequence of pro
CC sigma-K.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; X59528; CAA42107.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14757.1; -; Genomic_DNA.
DR PIR; S18438; S18438.
DR RefSeq; NP_390675.1; NC_000964.3.
DR RefSeq; WP_004398649.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P26937; -.
DR SMR; P26937; -.
DR DIP; DIP-48963N; -.
DR IntAct; P26937; 1.
DR STRING; 224308.BSU27970; -.
DR MEROPS; M50.002; -.
DR TCDB; 9.B.149.1.13; the m50 peptidase (m50-p) family.
DR PaxDb; P26937; -.
DR PRIDE; P26937; -.
DR EnsemblBacteria; CAB14757; CAB14757; BSU_27970.
DR GeneID; 937505; -.
DR KEGG; bsu:BSU27970; -.
DR PATRIC; fig|224308.179.peg.3039; -.
DR eggNOG; COG1994; Bacteria.
DR InParanoid; P26937; -.
DR OMA; EHGNRPF; -.
DR PhylomeDB; P26937; -.
DR BioCyc; BSUB:BSU27970-MON; -.
DR BRENDA; 3.4.21.116; 658.
DR BRENDA; 3.4.24.B23; 658.
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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR008915; Peptidase_M50.
DR Pfam; PF02163; Peptidase_M50; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..288
FT /note="Stage IV sporulation protein FB"
FT /id="PRO_0000088478"
FT TOPO_DOM 1..10
FT /note="Mother cell cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31
FT /note="Forespore intermembrane space"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..83
FT /note="Mother cell cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..126
FT /note="Forespore intermembrane space"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..161
FT /note="Mother cell cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179
FT /note="Forespore intermembrane space"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..288
FT /note="Mother cell cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 44
FT /evidence="ECO:0000305"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT MUTAGEN 43
FT /note="H->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10809718"
FT MUTAGEN 44
FT /note="E->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10809718"
FT MUTAGEN 44
FT /note="E->D: Partial activity."
FT /evidence="ECO:0000269|PubMed:10809718"
FT MUTAGEN 47
FT /note="H->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10809718"
SQ SEQUENCE 288 AA; 33640 MW; 81DB758DC215C916 CRC64;
MNKWLDLILK IHVHPFLWII AALGLLTGHM KALLCLLLIV LIHELGHAAL AVFFSWRIKR
VFLLPFGGTV EVEEHGNRPL KEEFAVIIAG PLQHIWLQFA AWMLAEVSVI HQHTFELFTF
YNLSILFVNL LPIWPLDGGK LLFLLFSKQL PFQKAHRLNL KTSLCFCLLL GCWVLFVIPL
QISAWVLFVF LAVSLFEEYR QRHYIHVRFL LERYYGKNRE LEKLLPLTVK AEDKVYHVMA
EFKRGCKHPI IIEKSGQKLS QLDENEVLHA YFADKRTNSS MEELLLPY
