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Database: UniProt
Entry: A5UMK9_METS3
LinkDB: A5UMK9_METS3
Original site: A5UMK9_METS3 
ID   A5UMK9_METS3            Unreviewed;       140 AA.
AC   A5UMK9;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Signal peptidase I {ECO:0000313|EMBL:ABQ87437.1};
DE            EC=3.4.21.89 {ECO:0000313|EMBL:ABQ87437.1};
GN   OrderedLocusNames=Msm_1232 {ECO:0000313|EMBL:ABQ87437.1};
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ87437.1, ECO:0000313|Proteomes:UP000001992};
RN   [1] {ECO:0000313|EMBL:ABQ87437.1, ECO:0000313|Proteomes:UP000001992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC   {ECO:0000313|Proteomes:UP000001992};
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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DR   EMBL; CP000678; ABQ87437.1; -; Genomic_DNA.
DR   RefSeq; WP_011954372.1; NZ_CP117965.1.
DR   AlphaFoldDB; A5UMK9; -.
DR   STRING; 420247.Msm_1232; -.
DR   MEROPS; S26.017; -.
DR   EnsemblBacteria; ABQ87437; ABQ87437; Msm_1232.
DR   GeneID; 78817885; -.
DR   KEGG; msi:Msm_1232; -.
DR   PATRIC; fig|420247.28.peg.1231; -.
DR   eggNOG; arCOG01739; Archaea.
DR   HOGENOM; CLU_089996_4_0_2; -.
DR   BioCyc; MSMI420247:GHWZ-1268-MONOMER; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR019533; Peptidase_S26.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR   PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR   PANTHER; PTHR10806:SF6; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00728; SIGNALPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABQ87437.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..82
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
SQ   SEQUENCE   140 AA;  15875 MW;  CACA3996772173AD CRC64;
     MTDYKEIISY IVILAVVLIA AQHLNVVVSG SMEPVFYRGD IVAVEKADFL GIHEFDPSDV
     RVGDIVVYDA TWYNEPVIHR VINITQINGT TYYMIKGDHN SHPDPYYATA DQINERVLTW
     DGHPIVIPYI GNISLWLRGL
//
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