ID A7GVM4_BACCN Unreviewed; 393 AA.
AC A7GVM4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:ABS24182.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ABS24182.1};
DE Flags: Precursor;
GN OrderedLocusNames=Bcer98_4001 {ECO:0000313|EMBL:ABS24182.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS24182.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS24182.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000764; ABS24182.1; -; Genomic_DNA.
DR RefSeq; WP_012096445.1; NC_009674.1.
DR AlphaFoldDB; A7GVM4; -.
DR STRING; 315749.Bcer98_4001; -.
DR GeneID; 56419547; -.
DR KEGG; bcy:Bcer98_4001; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_2_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002300; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:ABS24182.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..379
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 393 AA; 42329 MW; 804F82B9B3400D57 CRC64;
MSFIDEENRM KRTREKKHKG LVISSIAGTV VGASWFAFGA PLFSKSETKN MQQAEASEGN
IVNEPSQMMQ HSGFVDAVDR ASEAVVGVIN IQRDHFSEVD AEAGTGSGVI YKKTNGHAYI
VTNHHVIAGA NRIEISLSDG TKVPGKILGS DIVTDLAVIE INAKPVKKVI EIGDSNTVRR
GEAVIAIGNP LGLQFSGTVT QGIISANERI VPVDLDQDGH YDWQVEVLQT DAAINPGNSG
GALINAAGKL IGINSMKIAA KEVEGIGLAI PVTRAVPIMN ELEKYGTVRR PYIGIELRSL
NEIPNYYWEE TLHLPGGVTN GVCILDVKSP SPGAAAGLRE HDVIVAVDGK PIQDIIAFRT
ALYNKKIDDK MTLTFYRGTK RSTTTVKLAS QKY
//
