ID   A0A256A9T0_9FLAO        Unreviewed;       527 AA.
AC   A0A256A9T0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Peptidase C39 domain-containing protein {ECO:0000259|PROSITE:PS50990};
GN   ORFNames=CHX27_01170 {ECO:0000313|EMBL:OYQ49904.1};
OS   Flavobacterium aurantiibacter.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2023067 {ECO:0000313|EMBL:OYQ49904.1, ECO:0000313|Proteomes:UP000216035};
RN   [1] {ECO:0000313|EMBL:OYQ49904.1, ECO:0000313|Proteomes:UP000216035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH167 {ECO:0000313|EMBL:OYQ49904.1,
RC   ECO:0000313|Proteomes:UP000216035};
RA   Cai H.;
RT   "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT   aggregates in a eutrophic lake.";
RL   Submitted (JUL-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYQ49904.1}.
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; NOXX01000088; OYQ49904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256A9T0; -.
DR   OrthoDB; 1100563at2; -.
DR   Proteomes; UP000216035; 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; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR012932; VKOR.
DR   InterPro; IPR038354; VKOR_sf.
DR   Pfam; PF03412; Peptidase_C39; 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:UP000216035};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        133..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..120
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
SQ   SEQUENCE   527 AA;  60603 MW;  30443A9266483530 CRC64;
     MENKIVLLLY RFIQLNNYSI DLKTLQLQFL SHADYPSFRA ISDTLDYFNI QNIAAQIPVE
     AFDELPFPLI AILNNEDYSK ITVVEKKSDN NFVATDEKLT RKKLTKAELL RVWSGFIIAA
     EYSTEKVRKT DRYSISIITL VTLLSVFTLF VEYQNWVHLT YLLSSIVGCG ISWLIFKEKL
     GEKSLLVDKV CGLTNKKDGC AGIINDKSSN LIFGLTFSDA SMIYFSWITL TLVMFGYNAL
     AALVLGIFGL FVSIYSWYLQ GKVLKSWCSL CLGISSILIF QFITSIIMYR SPDFSLAHFL
     QIGVVFILVG IAWYYFSTQT FLQKDYNYLE ISATKFKRNQ SMFEMLLNKR SLKQPLSMLD
     DSVRFRFGST DPKIVITAVT NPLCGFCVET FQSYEKMLSK YSFLQLNLIF SVPNIQPDNP
     GVVVLRNVIE IYKLDGKESS LKSLSDWFML RDLNIWLKNY SRTFKMDSIK EVVLHHGSWI
     EENEITGTPT TIINNHFYPT EYKLSDFDFF ITEIKDSEEH SKAVVAV
//