ID A0A1G5ZAW7_9BACT Unreviewed; 342 AA.
AC A0A1G5ZAW7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Peptidase C39 family protein {ECO:0000313|EMBL:SDA92119.1};
GN ORFNames=SAMN03080617_03512 {ECO:0000313|EMBL:SDA92119.1};
OS Algoriphagus alkaliphilus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=279824 {ECO:0000313|EMBL:SDA92119.1, ECO:0000313|Proteomes:UP000198756};
RN [1] {ECO:0000313|EMBL:SDA92119.1, ECO:0000313|Proteomes:UP000198756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22703 {ECO:0000313|EMBL:SDA92119.1,
RC ECO:0000313|Proteomes:UP000198756};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the VKOR family.
CC {ECO:0000256|ARBA:ARBA00006214}.
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DR EMBL; FMXE01000031; SDA92119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5ZAW7; -.
DR STRING; 279824.SAMN03080617_03512; -.
DR Proteomes; UP000198756; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd12921; VKOR_4; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.1440.130; VKOR domain; 1.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF03412; Peptidase_C39; 1.
DR Pfam; PF07884; VKOR; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..126
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
SQ SEQUENCE 342 AA; 38168 MW; A34A5F7294CB28A1 CRC64;
MNFYYQSMEN CLIICKRLLE SLKVPFTGKF LKEKILTHPQ YPSLLSLSDT LEEYGVESVA
AKLGPERLDD FPLPGIVQVS LANGTFFNVI TAVSENMVSV FDEKGKQKDI SRLDFLKMWT
GVCLLVETKE NATEPEIGQK TRDQRIIRGL VVLGVVSFLL GLGLGLVENG SSGLFLFYFL
LKLLGLSISG VLLWYQQDKE NPTLQKFCSG GKSVDCNSVL DSKAFQLLDG RINPSMLASA
YFFAGLGLLV SSALFSMPFL AWLSMTTIPV VIYSFYYQGM VIKKWCRFCL LIQGVLVLEA
LAVLGGFLGR RAFFFSSWLV SFSFHWSGLG RRVDQTYAWT AG
//
