ID   A0A158CTB2_9BURK        Unreviewed;       408 AA.
AC   A0A158CTB2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:SAK85471.1};
GN   ORFNames=AWB79_05939 {ECO:0000313|EMBL:SAK85471.1};
OS   Caballeronia hypogeia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777140 {ECO:0000313|EMBL:SAK85471.1, ECO:0000313|Proteomes:UP000054851};
RN   [1] {ECO:0000313|Proteomes:UP000054851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; FCOA02000027; SAK85471.1; -; Genomic_DNA.
DR   RefSeq; WP_061170983.1; NZ_FCOA02000027.1.
DR   AlphaFoldDB; A0A158CTB2; -.
DR   STRING; 1777140.AWB79_05939; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000054851; 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   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          308..373
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          383..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        164
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   408 AA;  43041 MW;  246C8A8FB58E9922 CRC64;
     MLRRFWLFFA QAVTVLLALM FIIATLKPQW LQRQGQFGKQ LAAPIVALQE VAPSIGSRPV
     QSSYAEGAQK AMPAVVNVFS SKDGNLPPDP RAKDPLFRYF FGDKNKRKSD EPPASNLGSG
     VIVSSEGYIL TNQHVVDGAD QIEVALADGR TSSAKVIGVD PETDLAVLKV NMTNLPTITL
     GRMDQTRVGD VVLAIGNPFG VGQTVTMGIV SALGRNHLGI NTFENFIQTD AAINPGNSGG
     ALVDVNGNLL GINTAIYSRS GGSLGIGFAI PVSTARSVLE SIITTGSVTR GWIGVEPQDV
     TPEIAESFGL DQKSGAIVAG VLQGGPADKA GIKPGDILVS INDDTITDTT RLLNVVAQIK
     PGTSVKVHLM RKNKELDVNV MIGKRPAPPR APQMPDEDQG DGGDQGDE
//