ID A0A1Q1FJB9_9EURY Unreviewed; 300 AA.
AC A0A1Q1FJB9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=S49 family peptidase {ECO:0000313|EMBL:AQL42921.1};
GN ORFNames=BV210_09425 {ECO:0000313|EMBL:AQL42921.1};
OS Halorientalis sp. IM1011.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=1932360 {ECO:0000313|EMBL:AQL42921.1, ECO:0000313|Proteomes:UP000187924};
RN [1] {ECO:0000313|EMBL:AQL42921.1, ECO:0000313|Proteomes:UP000187924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM1011 {ECO:0000313|EMBL:AQL42921.1,
RC ECO:0000313|Proteomes:UP000187924};
RA Zhao D., Kumar S., Zhou J., Wang R., Xiang H.;
RT "Isolation and genome sequence of Halorientalis hydrocarbonoclasticus sp.
RT nov., a hydrocarbon-degrading haloarchaeon.";
RL Submitted (JAN-2017) 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; CP019067; AQL42921.1; -; Genomic_DNA.
DR RefSeq; WP_077206424.1; NZ_CP019067.1.
DR AlphaFoldDB; A0A1Q1FJB9; -.
DR STRING; 1932360.BV210_09425; -.
DR GeneID; 30959914; -.
DR KEGG; hali:BV210_09425; -.
DR OrthoDB; 27099at2157; -.
DR Proteomes; UP000187924; Chromosome.
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; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
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:UP000187924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..237
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 30676 MW; 939C2864748026D9 CRC64;
MSRDPGLLDR LGGPVVVFGV VGLVVGAALV PYAWGATTDP DGTVAVVEMH GTINGDTATA
AIEDLREARQ NDSIEAVVLD INSGGGLASV SEQLYLAVKR TSEQMPVKVA VTGMAASGAY
YMSAPADGIY VTPASTVGSV GVRAVVPQTG APDNQITTGP DKVTGATEDE ARQRVEALRR
AFVDSVVAER EDELNLSATE LSYAKVYSGT RSVELGLADE VGGLDAAVNA AAEDAGLSDY
RTVRKESPTP STLSSIGLNG SGGTASDGVT VETTQYLMLH GQLKTPDSGN VTEVSADGGN
//
