SP2G_BACTK
ID SP2G_BACTK Reviewed; 161 AA.
AC P26767;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Putative sporulation sigma factor-processing peptidase;
DE EC=3.4.23.-;
DE Flags: Fragment;
OS Bacillus thuringiensis subsp. kurstaki.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HD-1;
RX PubMed=1904859; DOI=10.1128/jb.173.12.3846-3854.1991;
RA Adams L.F., Brown K.L., Whiteley H.R.;
RT "Molecular cloning and characterization of two genes encoding sigma factors
RT that direct transcription from a Bacillus thuringiensis crystal protein
RT gene promoter.";
RL J. Bacteriol. 173:3846-3854(1991).
CC -!- FUNCTION: Probably activates the RNA polymerase sigma-35 factor at the
CC stage II of sporulation.
CC -!- SIMILARITY: Belongs to the peptidase U4 family. {ECO:0000305}.
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DR EMBL; X56697; CAA40025.1; -; Genomic_DNA.
DR PIR; D39441; D39441.
DR AlphaFoldDB; P26767; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030436; P:asexual sporulation; 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; IPR005081; SpoIIGA.
DR Pfam; PF03419; Peptidase_U4; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Hydrolase; Protease; Sporulation.
FT CHAIN <1..161
FT /note="Putative sporulation sigma factor-processing
FT peptidase"
FT /id="PRO_0000079180"
FT ACT_SITE 38
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 161 AA; 18182 MW; 09945F9F7F64FFBF CRC64;
FSKKRIESVE VTKIHYDQIV KVKIQLAEEE LELAGLIDSG NQLYDPLTKT PVMIMHVSSL
EHCLPSWLTE QIYSKTEIPQ IPENDSGWAT KLRLIPFRAV GVESQFLWAI KPDSVQVDHE
GSSIVVNKVL IGLNTQQLST NGEYQCIVHP KMLISQKMVI A