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Entry: F0S0K6_DESTD
LinkDB: F0S0K6_DESTD
Original site: F0S0K6_DESTD 
ID   F0S0K6_DESTD            Unreviewed;       217 AA.
AC   F0S0K6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   OrderedLocusNames=Dester_0075 {ECO:0000313|EMBL:ADY72734.1};
OS   Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Desulfurobacterium.
OX   NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY72734.1, ECO:0000313|Proteomes:UP000007102};
RN   [1] {ECO:0000313|EMBL:ADY72734.1, ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX   PubMed=22675590; DOI=10.4056/sigs.2465574;
RA   Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA   Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer
RT   Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT   hydrothermal vent.";
RL   Stand. Genomic Sci. 5:407-415(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; CP002543; ADY72734.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0S0K6; -.
DR   STRING; 868864.Dester_0075; -.
DR   MEROPS; S26.025; -.
DR   KEGG; dte:Dester_0075; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_3_0; -.
DR   InParanoid; F0S0K6; -.
DR   Proteomes; UP000007102; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:ADY72734.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007102}.
FT   DOMAIN          10..197
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   217 AA;  24992 MW;  2D58BEF5857A0297 CRC64;
     MEIAMQNKIV ENLKSFAIAL VLALIIRTFL VQSFHIPSGS MIPTLLVGDF ILVDKITYHL
     REPDRGDVVV FHFPLNEDVY YIKRIIGVPG DKVQVIDGKV YINGKPCKYE PGGTYSYTEK
     GSSYKGRLFY EFLPRKEGGE KKHLILKTGG RGDNTQVFVI PKDKYLMMGD NRNNSYDSRY
     WGFVDRSKIV GIARIIFFSW DGEKHLPRFN RIFKLIN
//
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