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Database: UniProt
Entry: L9W2G9_9EURY
LinkDB: L9W2G9_9EURY
Original site: L9W2G9_9EURY 
ID   L9W2G9_9EURY            Unreviewed;       331 AA.
AC   L9W2G9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Signal peptide peptidase SppA, 36K type {ECO:0000313|EMBL:ELY43704.1};
GN   ORFNames=C495_12869 {ECO:0000313|EMBL:ELY43704.1};
OS   Natronorubrum sulfidifaciens JCM 14089.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY43704.1, ECO:0000313|Proteomes:UP000011661};
RN   [1] {ECO:0000313|EMBL:ELY43704.1, ECO:0000313|Proteomes:UP000011661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY43704.1,
RC   ECO:0000313|Proteomes:UP000011661};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELY43704.1}.
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DR   EMBL; AOHX01000042; ELY43704.1; -; Genomic_DNA.
DR   RefSeq; WP_008163522.1; NZ_AOHX01000042.1.
DR   AlphaFoldDB; L9W2G9; -.
DR   STRING; 1230460.C495_12869; -.
DR   PATRIC; fig|1230460.4.peg.2618; -.
DR   eggNOG; arCOG01311; Archaea.
DR   OrthoDB; 31107at2157; -.
DR   Proteomes; UP000011661; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd07023; S49_Sppa_N_C; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR004635; Pept_S49_SppA.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR047272; S49_SppA_C.
DR   NCBIfam; TIGR00706; SppA_dom; 1.
DR   PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR   PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR   Pfam; PF01343; Peptidase_S49; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011661};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          141..281
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
SQ   SEQUENCE   331 AA;  35403 MW;  3077DB5BDF8CCEC6 CRC64;
     MASGRGIARL LIVVVGAAVF AVIGVSLFVV YPASMADLAG VLVALVVVVA GIRIAGSVAG
     SLFPGYDVAE VAVEGPITRD GGGGRLPSSP RGTPADDIVD QIDRADEDDN VDALLLKLNT
     PGGEIVPSDD IRLAAERFDG PTIAYTTDVC ASGGYWIASG CDELWARDGS IVGSIGVIGS
     RVNANDLAEK VGLSYERLAA GEYKDAGTPL KELEDDEREY LQGLIDDYYE TFVERVSDGR
     DLEPEFVRDT EARIYLGEEA YEMELVDHLG TRRELEDELA DRLDRDAVAV EAFEPERPLM
     ARIGTGAQQL AYAFGAGIAG IAEDREFRLR L
//
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