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Database: UniProt
Entry: B0K8L4_THEP3
LinkDB: B0K8L4_THEP3
Original site: B0K8L4_THEP3 
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
//
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