ID U5MNG3_CLOSA Unreviewed; 267 AA.
AC U5MNG3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 Name=spoIIGA {ECO:0000313|EMBL:AGX42344.1};
GN ORFNames=CLSA_c13410 {ECO:0000313|EMBL:AGX42344.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX42344.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX42344.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX42344.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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}.
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DR EMBL; CP006721; AGX42344.1; -; Genomic_DNA.
DR RefSeq; WP_022744626.1; NZ_AYXL01000317.1.
DR AlphaFoldDB; U5MNG3; -.
DR GeneID; 55473855; -.
DR KEGG; csb:CLSA_c13410; -.
DR PATRIC; fig|1345695.10.peg.3589; -.
DR eggNOG; ENOG50301AF; Bacteria.
DR HOGENOM; CLU_059158_0_0_9; -.
DR OrthoDB; 2690199at2; -.
DR Proteomes; UP000017118; Chromosome.
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, ECO:0000313|EMBL:AGX42344.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR018571, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PIRNR:PIRNR018571};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118};
KW Sporulation {ECO:0000256|PIRNR:PIRNR018571};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PIRSR:PIRSR018571-1"
SQ SEQUENCE 267 AA; 30471 MW; 4054E6D5018E253B CRC64;
MIIYVDVLIL ENFIVNLFLL TLTMRVIKHK SKLILLITSS FIGGMYTVVV IVPGLYFFRI
IPFEILIACI MLRIAYGKTN LINMIKLLGV FLGVTFMLSG ICFLFSLKQN IYILGNTFEI
QKYSIKYIMI GTMSIYIIYT RIADYVRERI FVSNYNFNVQ FIIGDKKYCL NGFLDTGNEL
REPITNLPCI LIEENIISDI GFEGKNTYSI PYNSIGYGGN LKGIRVNNIK IENKNFAYGL
IDAIICPCKE KMSGENEFNA LLPRGIV
//
