ID   A0A1Y5SZZ1_9RHOB        Unreviewed;       565 AA.
AC   A0A1Y5SZZ1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Serine protease Do-like HtrB {ECO:0000313|EMBL:SLN48921.1};
DE            EC=3.4.21.107 {ECO:0000313|EMBL:SLN48921.1};
GN   Name=htrB_2 {ECO:0000313|EMBL:SLN48921.1};
GN   ORFNames=TRL7639_02703 {ECO:0000313|EMBL:SLN48921.1};
OS   Falsiruegeria litorea R37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Falsiruegeria.
OX   NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN48921.1, ECO:0000313|Proteomes:UP000193077};
RN   [1] {ECO:0000313|EMBL:SLN48921.1, ECO:0000313|Proteomes:UP000193077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN48921.1,
RC   ECO:0000313|Proteomes:UP000193077};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWFO01000001; SLN48921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SZZ1; -.
DR   Proteomes; UP000193077; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:SLN48921.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SLN48921.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193077};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          162..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..192
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  58493 MW;  8B377A1A30C3F962 CRC64;
     MADQFLSKTK VTAGDLVTSG DRPVLERFDE LRALLTDRAG PEVANLFAEP LLSRGNDTAT
     PSVSWYANTK SDPVLLSQVS PGEQAQVTAY LSDHLRPLRA LAEEPAHADL VWGALSTYGA
     DDVMVADGRP VIVNWGLLPG GGGSSVSTRM AHFEATLGRY LTAPTRPPVE PSTTPAPAFT
     PQPAEPEHPP APPRRITPLA WAPLLVLLLL SGGVLFWLLQ PGTRLFPKQE PVITEQATLD
     AQRALNDELR ARADVLQAAL DGAVCRADGV LILPNGQTPE GLLPPKQGEA FPQTADAAPD
     ALLPNTTDRI VVQDPANPET PQTLLQTIEG RTVLVLAGTA NGLTAGSGFV VGPGLVVTNQ
     HVIEGAAPGQ LAVAGQAVGA PMAATPLKAT GPLADTGQDF ALLRVEGLNA PAFSLFQGDG
     SLKLNNVIAA GYPGDVLEID GDFAALQAGE AGAIPGLTVT DGIVNTEQKI GPETNVLMHS
     AALSSGNSGG PLVDMCGRVV GVNSFVRKGP LQNRGYALAV GDLLAFLQGT DAAPQVVDSP
     CQPTVRPFTA AAAPKDPAPA DPDKE
//