ID A0A0M0KPJ2_9BACI Unreviewed; 305 AA.
AC A0A0M0KPJ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=AMD01_20710 {ECO:0000313|EMBL:KOO40730.1};
OS Priestia koreensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO40730.1, ECO:0000313|Proteomes:UP000037558};
RN [1] {ECO:0000313|Proteomes:UP000037558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14210 dsm16467.";
RL Submitted (AUG-2015) 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:KOO40730.1}.
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DR EMBL; LILC01000032; KOO40730.1; -; Genomic_DNA.
DR RefSeq; WP_053403364.1; NZ_LILC01000032.1.
DR AlphaFoldDB; A0A0M0KPJ2; -.
DR STRING; 284581.AMD01_20710; -.
DR PATRIC; fig|284581.3.peg.1470; -.
DR OrthoDB; 2690199at2; -.
DR Proteomes; UP000037558; 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:UP000037558};
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..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..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 305 AA; 34375 MW; 6900121F30682DD7 CRC64;
MSVYLDVIWL LNFGLDTMLL VLCAIILKRR FKWWRMMIGG LFGSLIVIFM FTPLSQIMLH
PATKIATSVV MILTAFGYKR LRYLLENLLT FYFATFVVGG GLMGMHFLFT DMFISSGGEV
FTSSNAYGDP VSWLLVLLGS PLLFYFSKKR IEDVNMKTIT FDQLVQVEIM MNDTALTVDG
LLDSGNQLYD PLTKTPVMIV QADQLTDLLP ASIIESSANL KDFNFSIEPE WYNRIRLVPY
RSVGQSGQFL MAVKPDYVTI IQQGERIVAK QCLIGISHTQ LSPENLYQCV VHPKLLVSGK
ISSAS
//
