ID A0A095SGU0_9GAMM Unreviewed; 272 AA.
AC A0A095SGU0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=Y5S_02974 {ECO:0000313|EMBL:KGD63767.1};
OS Alcanivorax nanhaiticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD63767.1, ECO:0000313|Proteomes:UP000029444};
RN [1] {ECO:0000313|EMBL:KGD63767.1, ECO:0000313|Proteomes:UP000029444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19-m-6 {ECO:0000313|EMBL:KGD63767.1,
RC ECO:0000313|Proteomes:UP000029444};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:KGD63767.1}.
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DR EMBL; ARXV01000014; KGD63767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095SGU0; -.
DR STRING; 1177154.Y5S_02974; -.
DR PATRIC; fig|1177154.3.peg.3014; -.
DR eggNOG; COG0526; Bacteria.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000029444; Unassembled WGS sequence.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..268
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 272 AA; 29949 MW; 2AAC2421951529B0 CRC64;
MDAVIIGPLA LPAAAFITLI AFLTAVFSLQ WWQKRHHLAR SERALWLIAL SGLLGARLSF
LWRYQDQYPS LAAMLDIRDG GWWWPGGLLA IPVAVLLLWR TPNQRGGLLV ALSASAACTG
LAVVTLLALR QPTTPLPDVA LYTLQGEPVP LQQVSAGQLT LINLWASWCP PCRREMPVLQ
DAQSRYPPLR ILLANQGETS ASVRRYLTEQ ELQFDFSLLD PNTELSRHTG NSGLPLTLLV
DAQGNELARH FGPLSAASLH HFLQPHLPGD PQ
//
