ID R6MUI5_9FIRM Unreviewed; 265 AA.
AC R6MUI5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BN531_01584 {ECO:0000313|EMBL:CDC02435.1};
OS Eubacterium sp. CAG:202.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262884 {ECO:0000313|EMBL:CDC02435.1, ECO:0000313|Proteomes:UP000017996};
RN [1] {ECO:0000313|EMBL:CDC02435.1, ECO:0000313|Proteomes:UP000017996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:202 {ECO:0000313|Proteomes:UP000017996};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CDC02435.1}.
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DR EMBL; CBEO010000114; CDC02435.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MUI5; -.
DR STRING; 1262884.BN531_01584; -.
DR Proteomes; UP000017996; 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 Pfam; PF03419; Peptidase_U4; 1.
DR PIRSF; PIRSF018571; SpoIIGA; 2.
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:UP000017996};
KW Sporulation {ECO:0000256|PIRNR:PIRNR018571};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR018571-1"
SQ SEQUENCE 265 AA; 29725 MW; E3E7D8669BE8D25A CRC64;
MNNIYIDVLI TVNIFIDYFL LMLTKKIIGS NIKYFRVIIG SIVGGLFSLT ALLPVLPFGL
NILTDLAVAM LIIFITFGKC KIKTYIKRVL IFFALSFSFG GLMIFIYLAF KPKGMGIYND
VIYFDISPVL LIILTLVCYY ILLLIKKLTK SVYKSDIHNI EIKINDKCYI FNAKLDTGCN
VKEPFSGKSV IVAEKEVFND FVPDKTKVRL IPFTSLGGSG ILQGFCADNI IIDGKEADNS
VYIGICENIF KDDIKAIIPS ELINN
//
