SP2G_BACSU
ID SP2G_BACSU Reviewed; 309 AA.
AC P13801;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sporulation sigma-E factor-processing peptidase;
DE EC=3.4.23.-;
DE AltName: Full=Membrane-associated aspartic protease;
DE AltName: Full=Stage II sporulation protein GA;
GN Name=spoIIGA; OrderedLocusNames=BSU15310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168;
RX PubMed=3125985; DOI=10.1016/0092-8674(88)90407-2;
RA Stragier P., Bonamy C., Karmazyn-Campelli C.;
RT "Processing of a sporulation sigma factor in Bacillus subtilis: how
RT morphological structure could control gene expression.";
RL Cell 52:697-704(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2106671; DOI=10.1093/nar/18.3.657;
RA Masuda E.S., Anaguchi H., Sato T., Takeuchi M., Kobayashi Y.;
RT "Nucleotide sequence of the sporulation gene spoIIGA from Bacillus
RT subtilis.";
RL Nucleic Acids Res. 18:657-657(1990).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1744037; DOI=10.1128/jb.173.24.7821-7827.1991;
RA Peters H.K. III, Haldenwang W.G.;
RT "Synthesis and fractionation properties of SpoIIGA, a protein essential for
RT pro-sigma E processing in Bacillus subtilis.";
RL J. Bacteriol. 173:7821-7827(1991).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PRO-259.
RX PubMed=8002606; DOI=10.1128/jb.176.24.7763-7766.1994;
RA Peters H.K. III, Haldenwang W.G.;
RT "Isolation of a Bacillus subtilis spoIIGA allele that suppresses
RT processing-negative mutations in the Pro-sigma E gene (sigE).";
RL J. Bacteriol. 176:7763-7766(1994).
RN [6]
RP FUNCTION.
RX PubMed=7585939; DOI=10.1016/0092-8674(95)90163-9;
RA Hofmeister A.E., Londono-Vallejo A., Harry E., Stragier P., Losick R.;
RT "Extracellular signal protein triggering the proteolytic activation of a
RT developmental transcription factor in B. subtilis.";
RL Cell 83:219-226(1995).
RN [7]
RP INTERACTION WITH SIGE, AND DISRUPTION PHENOTYPE.
RX PubMed=9573195; DOI=10.1128/jb.180.9.2426-2433.1998;
RA Hofmeister A.;
RT "Activation of the proprotein transcription factor pro-sigmaE is associated
RT with its progression through three patterns of subcellular localization
RT during sporulation in Bacillus subtilis.";
RL J. Bacteriol. 180:2426-2433(1998).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9663680; DOI=10.1046/j.1365-2958.1998.00849.x;
RA Fawcett P., Melnikov A., Youngman P.;
RT "The Bacillus SpoIIGA protein is targeted to sites of spore septum
RT formation in a SpoIIE-independent manner.";
RL Mol. Microbiol. 28:931-943(1998).
RN [9]
RP FUNCTION, INTERACTION WITH SPOIIR, SUBUNIT, SUBCELLULAR LOCATION, ACTIVE
RP SITE, AND MUTAGENESIS OF ARG-164; VAL-165; HIS-177; GLY-180; LEU-181;
RP ILE-182; ASP-183; SER-184; GLY-185; ASP-190; ASP-230; GLN-252; ASP-260;
RP HIS-261; THR-282; THR-283; SER-286; ILE-294; ILE-295; HIS-296; LYS-298;
RP 302-GLY--SER-309 AND HIS-307.
RX PubMed=18378688; DOI=10.1074/jbc.m708962200;
RA Imamura D., Zhou R., Feig M., Kroos L.;
RT "Evidence that the Bacillus subtilis SpoIIGA protein is a novel type of
RT signal-transducing aspartic protease.";
RL J. Biol. Chem. 283:15287-15299(2008).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-183; ARG-245; PRO-259 AND LYS-284.
RX PubMed=21362630; DOI=10.1093/jb/mvr027;
RA Imamura D., Kuwana R., Kroos L., Feig M., Takamatsu H., Watabe K.;
RT "Substrate specificity of SpoIIGA, a signal-transducing aspartic protease
RT in Bacilli.";
RL J. Biochem. 149:665-671(2011).
CC -!- FUNCTION: Probable aspartic protease that is responsible for the
CC proteolytic cleavage of the RNA polymerase sigma E factor
CC (SigE/spoIIGB) to yield the active peptide in the mother cell during
CC sporulation. Responds to a signal from the forespore that is triggered
CC by the extracellular signal protein SpoIIR.
CC {ECO:0000269|PubMed:1744037, ECO:0000269|PubMed:18378688,
CC ECO:0000269|PubMed:21362630, ECO:0000269|PubMed:3125985,
CC ECO:0000269|PubMed:7585939, ECO:0000269|PubMed:8002606}.
CC -!- SUBUNIT: Self-associates. Interacts with SigE (Probable). Interacts
CC with SpoIIR. {ECO:0000269|PubMed:18378688, ECO:0000269|PubMed:9573195,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1744037,
CC ECO:0000269|PubMed:18378688, ECO:0000269|PubMed:9663680}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:1744037,
CC ECO:0000269|PubMed:18378688, ECO:0000269|PubMed:9663680}.
CC Note=Localized to the sporulation septum.
CC -!- DISRUPTION PHENOTYPE: Does not affect the localization of SigE.
CC {ECO:0000269|PubMed:9573195}.
CC -!- SIMILARITY: Belongs to the peptidase U4 family. {ECO:0000305}.
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DR EMBL; X17344; CAA35225.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13405.1; -; Genomic_DNA.
DR PIR; S08224; A29812.
DR RefSeq; NP_389414.1; NC_000964.3.
DR RefSeq; WP_003232163.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P13801; -.
DR STRING; 224308.BSU15310; -.
DR MEROPS; A36.001; -.
DR PaxDb; P13801; -.
DR PRIDE; P13801; -.
DR DNASU; 939984; -.
DR EnsemblBacteria; CAB13405; CAB13405; BSU_15310.
DR GeneID; 939984; -.
DR KEGG; bsu:BSU15310; -.
DR PATRIC; fig|224308.179.peg.1669; -.
DR eggNOG; ENOG50301AF; Bacteria.
DR OMA; IYLDVIW; -.
DR BioCyc; BSUB:BSU15310-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IMP:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0030436; P:asexual sporulation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR005081; SpoIIGA.
DR Pfam; PF03419; Peptidase_U4; 1.
DR PIRSF; PIRSF018571; SpoIIGA; 1.
DR TIGRFAMs; TIGR02854; spore_II_GA; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Sporulation sigma-E factor-processing peptidase"
FT /id="PRO_0000079179"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000305|PubMed:18378688"
FT MUTAGEN 164
FT /note="R->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 164
FT /note="R->I: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 164
FT /note="R->K: 75% reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 165
FT /note="V->A,P: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 177
FT /note="H->A: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 180
FT /note="G->A: 70% reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 180
FT /note="G->D: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 181
FT /note="L->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 182
FT /note="I->A,D: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 183
FT /note="D->A: Abolishes cleavage of wild-type SigE.
FT Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688,
FT ECO:0000269|PubMed:21362630"
FT MUTAGEN 183
FT /note="D->E,N: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688,
FT ECO:0000269|PubMed:21362630"
FT MUTAGEN 184
FT /note="S->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 184
FT /note="S->C: 2-fold reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 184
FT /note="S->T: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 185
FT /note="G->A: 60% reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 185
FT /note="G->V: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 190
FT /note="D->E: 2-fold reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 230
FT /note="D->E: 2-fold reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 245
FT /note="R->D: Abolishes cleavage of SigE."
FT /evidence="ECO:0000269|PubMed:21362630"
FT MUTAGEN 252
FT /note="Q->E: 60% reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 259
FT /note="P->L: Unaffected cleavage of wild-type and K-25
FT mutant SigE in sporulating B.subtilis cells
FT (PubMed:8002606). Abolishes cleavage of wild-type and K-25
FT mutant SigE when proteins are coexpressed in E.coli cells
FT (PubMed:21362630)."
FT /evidence="ECO:0000269|PubMed:21362630,
FT ECO:0000269|PubMed:8002606"
FT MUTAGEN 260
FT /note="D->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 260
FT /note="D->E: 2-fold reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 261
FT /note="H->A,S: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 282
FT /note="T->E: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 283
FT /note="T->A: Nearly unaffected cleavage of SigE I-17
FT mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 284
FT /note="K->D: Reduced cleavage of SigE."
FT /evidence="ECO:0000269|PubMed:21362630"
FT MUTAGEN 286
FT /note="S->A: 80% reduced cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 294
FT /note="I->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 295
FT /note="I->A: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 296
FT /note="H->A,E,F,G,I,Q,S: Abolishes cleavage of SigE I-17
FT mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 296
FT /note="H->G: Abolishes cleavage of SigE I-17 mutant; when
FT associated with N-298."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 298
FT /note="K->A: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 298
FT /note="K->N: 80% reduced cleavage of SigE I-17 mutant.
FT Abolishes cleavage of SigE I-17 mutant; when associated
FT with G-296."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 302..309
FT /note="Missing: Abolishes cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
FT MUTAGEN 307
FT /note="H->A: Unaffected cleavage of SigE I-17 mutant."
FT /evidence="ECO:0000269|PubMed:18378688"
SQ SEQUENCE 309 AA; 34857 MW; 7B3453BA582C04EB CRC64;
MKIYLDVIWL LNFCFDALLL LLTAFILKRH VKKRRLVGGA FIGSSIVLLM FTPFSPIVEH
PAGKLAFSVV IVVVTFGFKR FRFFFQNLFS FYFATFLMGG GIIGAHSLLQ SNSIVQNGVM
ITNQTGFGDP ISWLFIVGGF PALWFFSKRR IEDIETKNIQ YEERVSVQAD LGSQTLHVRG
LIDSGNQLYD PLTKTPVMII YIDKLEPIFG TAETMIIRNT DPLEAIEQLD DSFRFLDKMR
LIPYRGVGQQ NQFLLCVKPD HVTIMTKEEM ISADKCLIGI STTKLSADGE FDAIIHPKML
SGKAVKHVS
