ID   A0A1G9QPZ9_9EURY        Unreviewed;       332 AA.
AC   A0A1G9QPZ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protease-4 {ECO:0000313|EMBL:SDM13122.1};
GN   ORFNames=SAMN04487949_0974 {ECO:0000313|EMBL:SDM13122.1};
OS   Halogranum gelatinilyticum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=660521 {ECO:0000313|EMBL:SDM13122.1, ECO:0000313|Proteomes:UP000199451};
RN   [1] {ECO:0000313|Proteomes:UP000199451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10119 {ECO:0000313|Proteomes:UP000199451};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
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DR   EMBL; FNHL01000001; SDM13122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9QPZ9; -.
DR   STRING; 660521.SAMN04487949_0974; -.
DR   OrthoDB; 31107at2157; -.
DR   Proteomes; UP000199451; 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:UniProtKB-KW.
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, ECO:0000313|EMBL:SDM13122.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SDM13122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199451};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          142..281
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
SQ   SEQUENCE   332 AA;  35305 MW;  657B725B9B84CFCD CRC64;
     MSDRSTRIVQ LLIVLVAVAV AAVVGWLLFY AVPDDIAELL GVLLTIALVV FGARAGSRLA
     SRRYPDYNVA EVAVEGPISR DGGPGRLPTS PGGASADEIA DLVEAADEDD NVQALLVKLD
     TPGGAVVPSD DIRRAAAAFD GPTVAYTTDV CASGGYWIAS GCDELWAREG SIVGSIGVIG
     SRPNVSELAD QLGVSYERFA AGKYKDAGQP LKEMSDDERS YLQGIVDDYY EHFVERVAEG
     RDMDPEAIRE TEARVYLGTE ALELGLVDQL GTREEVEDHV ADRIGEEVSV SEFQPDRGLT
     SRLRGGSQAV AYALGAGVAS AVDPDDGFDF RF
//