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Database: UniProt
Entry: G7WHC0_DESOD
LinkDB: G7WHC0_DESOD
Original site: G7WHC0_DESOD 
ID   G7WHC0_DESOD            Unreviewed;       305 AA.
AC   G7WHC0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=Desor_4809 {ECO:0000313|EMBL:AET70210.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET70210.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET70210.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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; CP003108; AET70210.1; -; Genomic_DNA.
DR   RefSeq; WP_014187016.1; NC_016584.1.
DR   AlphaFoldDB; G7WHC0; -.
DR   STRING; 768706.Desor_4809; -.
DR   KEGG; dor:Desor_4809; -.
DR   PATRIC; fig|768706.3.peg.4891; -.
DR   eggNOG; ENOG50301AF; Bacteria.
DR   HOGENOM; CLU_059158_0_0_9; -.
DR   Proteomes; UP000006346; 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; 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:UP000006346};
KW   Sporulation {ECO:0000256|PIRNR:PIRNR018571};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018571-1"
SQ   SEQUENCE   305 AA;  34340 MW;  722E1C7614450119 CRC64;
     MSAAETYLDL VILINGGMDA LVLVLLGKLL HLPSRPMRII TAALVGEIPV LLACYSISPW
     TTISKWLIPF LMVIVAYPTK RPGTFLKALV GFWLLSAGLG GFMYGLWGWT KFDDGLEKEN
     LILIVHDLWV LPLGALLWWL LQNFWQRWQE RKAMLERTIY DLEICFGGEE NGTVHIKALL
     DTGNDLRDPL TGSPVILLEE EAAAKAIPAS VKAFMDIPWK DCPDPWPLLW KLNPNLIKRL
     VFIPFQTIDA KSWLLGIRPE HVTFCESKES RQIHATVALV KQVLSLEGEY QALLHPEHVQ
     KGGDG
//
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