SP2G_PRIM1
ID SP2G_PRIM1 Reviewed; 307 AA.
AC D5DQW6; O52061;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Sporulation sigma-E factor-processing peptidase {ECO:0000250|UniProtKB:P13801, ECO:0000312|EMBL:ADE71281.1};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:P13801, ECO:0000312|EMBL:ADE71281.1};
DE AltName: Full=Membrane-associated aspartic protease {ECO:0000250|UniProtKB:P13801};
DE AltName: Full=Stage II sporulation protein GA {ECO:0000250|UniProtKB:P13801};
GN Name=spoIIGA {ECO:0000312|EMBL:ADE71281.1}; OrderedLocusNames=BMQ_4271;
OS Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=545693;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB94055.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 12872 / QMB1551 {ECO:0000269|PubMed:9663680};
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 [2] {ECO:0000312|EMBL:ADE71281.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551;
RX PubMed=21705586; DOI=10.1128/jb.00449-11;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA Bremer E., Jahn D., Ravel J., Vary P.S.;
RT "Genome sequences of the biotechnologically important Bacillus megaterium
RT strains QM B1551 and DSM319.";
RL J. Bacteriol. 193:4199-4213(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 (By similarity).
CC {ECO:0000250|UniProtKB:P13801}.
CC -!- SUBUNIT: Self-associates. Interacts with SigE. Interacts with SpoIIR
CC (By similarity). {ECO:0000250|UniProtKB:P13801}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9663680};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9663680}.
CC Note=Localized to the sporulation septum. Early in sporulating cells
CC localized in an annulus at the septal periphery and later localized
CC uniformly throughout the septa. {ECO:0000269|PubMed:9663680}.
CC -!- SIMILARITY: Belongs to the peptidase U4 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADE71281.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF017181; AAB94055.1; -; Genomic_DNA.
DR EMBL; CP001983; ADE71281.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041816622.1; NC_014019.1.
DR AlphaFoldDB; D5DQW6; -.
DR STRING; 545693.BMQ_4271; -.
DR MEROPS; A36.001; -.
DR EnsemblBacteria; ADE71281; ADE71281; BMQ_4271.
DR KEGG; bmq:BMQ_4271; -.
DR eggNOG; ENOG50301AF; Bacteria.
DR HOGENOM; CLU_059158_0_0_9; -.
DR OrthoDB; 1492550at2; -.
DR Proteomes; UP000000935; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Pfam; PF03419; Peptidase_U4; 1.
DR PIRSF; PIRSF018571; SpoIIGA; 1.
DR TIGRFAMs; TIGR02854; spore_II_GA; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..307
FT /note="Sporulation sigma-E factor-processing peptidase"
FT /id="PRO_0000429023"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:P13801"
FT CONFLICT 25
FT /note="V -> A (in Ref. 1; AAB94055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35146 MW; 8B46801371E4E7B2 CRC64;
MPIYLDLIWM LNFGLDTILL MLCAVVLKRN YKWWRLLLGG FIGSLIVLLM FTPFSHLMVH
PAIKILFSFF MVLMTFGYKR LRFFFENLLT FYFATFVVGG GLMGVHFLFQ DQFLVLNQMV
DTKSPQFGDP ISWIFVLIGF PLLSYFSKTR VDDLRIKNIT FDQLVDVEII LNEQTLSMKG
LIDSGNQLVD PLTKTPVMIV TADSLKEILP EGLMELSKNV QSFSHSEDID QEWYSKVRFV
PYRSVGQANQ LLLALKPDMV RLVHQSNTIE VTKVLVGISH TTLSVEKQYE CIVHPKLIVI
GEVSSAS
