ID A0A919WXU5_9BACI Unreviewed; 308 AA.
AC A0A919WXU5;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 6.
DE RecName: Full=Sporulation sigma-E factor-processing peptidase {ECO:0000256|PIRNR:PIRNR018571};
DE EC=3.4.23.- {ECO:0000256|PIRNR:PIRNR018571};
DE AltName: Full=Membrane-associated aspartic protease {ECO:0000256|PIRNR:PIRNR018571};
DE AltName: Full=Stage II sporulation protein GA {ECO:0000256|PIRNR:PIRNR018571};
GN ORFNames=J14TS2_48400 {ECO:0000313|EMBL:GIN74365.1};
OS Bacillus sp. J14TS2.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2807188 {ECO:0000313|EMBL:GIN74365.1, ECO:0000313|Proteomes:UP000677829};
RN [1] {ECO:0000313|EMBL:GIN74365.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J14TS2 {ECO:0000313|EMBL:GIN74365.1};
RA Okamoto M., Kumagai M., Kanamori H., Takamatsu D.;
RT "Antimicrobial resistance genes in bacteria isolated from Japanese honey,
RT and their potential for conferring macrolide and lincosamide resistance in
RT the American foulbrood pathogen Paenibacillus larvae.";
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR018571}.
CC -!- SUBUNIT: Self-associates. Interacts with SigE. Interacts with SpoIIR.
CC {ECO:0000256|PIRNR:PIRNR018571}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR018571}.
CC -!- SIMILARITY: Belongs to the peptidase U4 family.
CC {ECO:0000256|PIRNR:PIRNR018571}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GIN74365.1}.
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DR EMBL; BORE01000022; GIN74365.1; -; Genomic_DNA.
DR RefSeq; WP_212975914.1; NZ_BORE01000022.1.
DR Proteomes; UP000677829; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 NCBIfam; TIGR02854; spore_II_GA; 1.
DR Pfam; PF03419; Peptidase_U4; 1.
DR PIRSF; PIRSF018571; SpoIIGA; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|PIRNR:PIRNR018571};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR018571};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR018571};
KW Membrane {ECO:0000256|PIRNR:PIRNR018571, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PIRNR:PIRNR018571};
KW Reference proteome {ECO:0000313|Proteomes:UP000677829};
KW Sporulation {ECO:0000256|PIRNR:PIRNR018571};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PIRSR:PIRSR018571-1"
SQ SEQUENCE 308 AA; 34722 MW; 100896700075C90D CRC64;
MVVYLDIIWL LNFIIDSFLL WATSIYLKRK IHPFKIIIGG LIGSLIILMA ATPISTWAMH
PFIKWSLSIV MIGITFGYKR LSTFVASLFT FYFATFLMGG ILIGTHYFLS FHLDLRNSVA
IESVRGYGDP ISWLFVAVAF PIAWFFSKKR IGHLTKTSIQ YDVLYDVFIL MNGIELKLKG
LIDSGNQLYD PISKKPVMIV SIESVKDKLP EELQNIADAQ DDLYTASTLL PTDWAHIMRL
IPAKTLGKNN QLLCAFKPEK VVIQEESGRE IEKEVLLVFT SQLLSGDGTF QCILHPQMAP
SLAMDSAS
//
