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Database: UniProt
Entry: A0A1B3W6Y4_9GAMM
LinkDB: A0A1B3W6Y4_9GAMM
Original site: A0A1B3W6Y4_9GAMM 
ID   A0A1B3W6Y4_9GAMM        Unreviewed;       277 AA.
AC   A0A1B3W6Y4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Redoxin {ECO:0000313|EMBL:AOH35835.1};
GN   ORFNames=BGP89_05255 {ECO:0000313|EMBL:AOH35835.1};
OS   Luteimonas sp. JM171.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Luteimonas.
OX   NCBI_TaxID=1896164 {ECO:0000313|EMBL:AOH35835.1, ECO:0000313|Proteomes:UP000095036};
RN   [1] {ECO:0000313|Proteomes:UP000095036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM171 {ECO:0000313|Proteomes:UP000095036};
RA   Wan X., Miller J.M., Rowley S.J., Hou S., Donachie S.P.;
RT   "Draft genome sequence of a novel Luteimonas sp. from coral mucus,
RT   Hawaii.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017074; AOH35835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B3W6Y4; -.
DR   STRING; 1896164.BGP89_05255; -.
DR   OrthoDB; 9796554at2; -.
DR   Proteomes; UP000095036; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001640; Lgt.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF01790; LGT; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095036};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          131..273
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   277 AA;  29601 MW;  5EE9AFAFCFE22D9E CRC64;
     MMGVGPFPIR AVVVALAALV AWAVARALAR RLPGSPVKPA GAMVVDALFI GLLVARLAFV
     VAWWREYAAA PLTIIQIGDG GFVWWAGLAA GIGFVAWRTR AAAALRRPVL AGIAAGTLAW
     GAAGGALWWM QYSASPMPDV ALADLEGRPV DLGEYSGRPV VLNMWATWCP PCRREMPVIE
     RAQAAYPDVS FVLVNQGEDA QTIQRFLADE GLQLDNILRD PHSRTMAETG ARALPTTLYF
     SPDGRLVDSH MGELTGASLA DTLGRQFGAR PVSNPME
//
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