ID B0K8L4_THEP3 Unreviewed; 276 AA.
AC B0K8L4;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=Teth39_0820 {ECO:0000313|EMBL:ABY94477.1};
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94477.1, ECO:0000313|Proteomes:UP000002156};
RN [1] {ECO:0000313|Proteomes:UP000002156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E
RC {ECO:0000313|Proteomes:UP000002156};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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}.
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DR EMBL; CP000924; ABY94477.1; -; Genomic_DNA.
DR RefSeq; WP_012269189.1; NC_010321.1.
DR AlphaFoldDB; B0K8L4; -.
DR STRING; 340099.Teth39_0820; -.
DR KEGG; tpd:Teth39_0820; -.
DR eggNOG; ENOG50301AF; Bacteria.
DR HOGENOM; CLU_059158_0_0_9; -.
DR Proteomes; UP000002156; 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 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:UP000002156};
KW Sporulation {ECO:0000256|PIRNR:PIRNR018571};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..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 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR018571-1"
SQ SEQUENCE 276 AA; 31942 MW; 75C4B1F39CEF9542 CRC64;
MYLDVIFFEN LIINYLILSL TRKFSKKGSK PIKLFLGALL GACYVLIFFL LPYKMIHEVF
AKIILSLLII YMAFTPKTLK EFLRILAVFY LISFAIGGTI FAVLYTAKFN LHSLWIGILI
AILLFYTNWD YIVRKSKEEK MLYSIKIEIF QKQVEIKGLL DTGNRLYDPL TKSPVVVVEF
LAMKNILPDN MEILLNEEKI DFNKIFEVLK EERWLSRIRL IPFISVGQSK GIMLGFKPDK
LVVGEKEIRN VIVGVYKSQI DKYGNYAALL APEILV
//