ID   A0A1I3CVP7_9GAMM        Unreviewed;       358 AA.
AC   A0A1I3CVP7;
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:SFH78456.1};
GN   ORFNames=SAMN04487959_109114 {ECO:0000313|EMBL:SFH78456.1};
OS   Halomonas xianhensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH78456.1, ECO:0000313|Proteomes:UP000199040};
RN   [1] {ECO:0000313|EMBL:SFH78456.1, ECO:0000313|Proteomes:UP000199040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH78456.1,
RC   ECO:0000313|Proteomes:UP000199040};
RA   de Groot N.N.;
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; FOPY01000009; SFH78456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3CVP7; -.
DR   STRING; 442341.SAMN04487959_109114; -.
DR   Proteomes; UP000199040; 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   Gene3D; 6.20.330.10; -; 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:SFH78456.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFH78456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199040};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        72..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..311
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  39984 MW;  7E1C7629E86ED8B3 CRC64;
     MSDDKRYDQW TEGPEVSREE ADAQLEQGAV PSSGRDDADT LRERQRLAQL EMMDRWIEGV
     LTEQRRSRRW KLFFRFFFAA LILASLSLSI YSLFLADMTP SPIGQHLGVV RVEGVIDAEA
     EANADRIIEG LRRAWSSPET AAVVVRINSP GGSPVQSQRV YQEIRRIRDA GDKPVYAIIE
     DIGASGAYYM AAAADDIYAA PASMVGSIGV IYAGFGLEQA IERLGVERRV FTAGENKAFL
     DPFSDIAPDQ RQFWQQVLET THQQFIEDVK VGRGDRLADD PRLFSGLVWT GEQAQALGLV
     DGLKSLDQLA RERLGEVRTR DYTPGLDPFE KLSRQFGRVA AQWLGVPQAS SPVRYELP
//