ID A0A0G3BR02_9BURK Unreviewed; 394 AA.
AC A0A0G3BR02;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=AAW51_5158 {ECO:0000313|EMBL:AKJ31849.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ31849.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ31849.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ31849.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP011371; AKJ31849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3BR02; -.
DR STRING; 413882.AAW51_5158; -.
DR KEGG; pbh:AAW51_5158; -.
DR PATRIC; fig|413882.6.peg.5386; -.
DR Proteomes; UP000035352; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03012; TlpA_like_DipZ_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852:SF13; PROTEIN DIPZ; 1.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035352};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..390
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 394 AA; 41165 MW; A81B26C11D5082DF CRC64;
MAAPLLQLGL AAGAGVATVA SPCVLPMLPM LLGGSIGQAD RLRPLLIVAG FVLSFATLAL
VFGASAQALG VSAASVRQAA AVVMLLAGLL MLWPALGDRL SVSLQPLGQW GHRVAGIATG
RRLGAFLLGA ALGALWAPCA GPVLASILAL IAQARPGEAA PLLAAFAVGA AAPMLAIGYG
GQAASLRMRA MARHTGRLRR AFGLAVVAVA VAMLAKVDTQ VVAALSRWVS AGAAAAVQPE
ADGPVPVGAP APDFAGITHW LNSPPLTMSQ LRGRVVLVDF WTYGCVNCVR TLPHVRRWHE
RYAADGLVVV GVHTPEFGHE RPLQNVQAAV QRHGLRYPVA QDNGYATWSA YRNVYWPALY
LVDRDGRIVF RHFGEGDEAQ VEQRLRQALG LAPS
//
