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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//