ID A0A1G7NG63_9SPHI Unreviewed; 555 AA.
AC A0A1G7NG63;
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=Uncharacterized membrane protein {ECO:0000313|EMBL:SDF72299.1};
GN ORFNames=SAMN05216464_12631 {ECO:0000313|EMBL:SDF72299.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDF72299.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDF72299.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDF72299.1,
RC ECO:0000313|Proteomes:UP000199072};
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; FNAI01000026; SDF72299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7NG63; -.
DR STRING; 1391627.SAMN05216464_12631; -.
DR OrthoDB; 1100563at2; -.
DR Proteomes; UP000199072; 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; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.20.1440.130; VKOR domain; 1.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF03412; Peptidase_C39; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR Pfam; PF07884; VKOR; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000199072};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..132
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
SQ SEQUENCE 555 AA; 62466 MW; CE203E139824E2D9 CRC64;
MQHYLSRILE PKVNGPETAS LLVNLLKVKL SDSTLKKEIE EHPEYPSLLS ISDVLNKYGI
DNLGIKFDNE KFSEIPTPFI TQIKHEVRPT NLFTVVKENG DNVVFFDPEK KRWNKLNKNA
FLKRCSGIAL LAEANDNAGE KDYKIKIKEE RQKRATQYFS VGGVPALFII VCLAGFMQSG
ISALLPFIFS LLTLAGCLSG VLLLWYELDQ YNPLIRKICS AGKKTNCSAV LHSKASKIAG
ISWSVIGFTY FAGMLLLLLF SGLTNLSVLS VLSWINVLAL PYTIFSIYYQ WRIAKQWCIL
CLSVQTLLVL QAVIAFTGGW HNVVSFNSID VGLIAKVIVS FSVPFIIAIV LLPALQKAKL
GNRFSNELQR LKHNAQIFSA LLEKQRPVIT DPSGLGITLG NPDAAYKIIK VCSPYCGPCA
EAHKPMEALL HHNSNIQLQI LYATGSDEDN ILKPPVKHFL AIAENNNEEI IKQALGDWYE
TKEKDYDMFA VKYPMNGELK KQDVKMEAMR NWCTKNEISY TPTIYISMPH DSGEVKYYEM
PGVYSFDDLN YFFRA
//