ID V4RR79_9CAUL Unreviewed; 268 AA.
AC V4RR79;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=ABENE_05025 {ECO:0000313|EMBL:ESQ93683.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ93683.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ93683.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ93683.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ93683.1}.
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DR EMBL; AWGB01000007; ESQ93683.1; -; Genomic_DNA.
DR RefSeq; WP_018081706.1; NZ_AWGB01000007.1.
DR AlphaFoldDB; V4RR79; -.
DR STRING; 1121022.GCA_000376105_02042; -.
DR PATRIC; fig|1121022.4.peg.999; -.
DR eggNOG; COG0526; Bacteria.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000017837; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
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; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000017837};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..267
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 268 AA; 29358 MW; ADD5F856C3B7279A CRC64;
MTEPKLNENG QPQPQSPAQA DIQGQPATGP VVKPIDEPVA EPKTGDTEKW RDTAIVRKRR
RPPLAVVIVV SVVVLTLIGL IGWRFLAPKA APLAALTAAQ SLAPVETARG PLAVYAKGAM
AKLVTYETPQ TIENIFFLDR EQKPVQLTDF KGQVVVLNVW ATWCAPCRFE MPTLAHLQTL
YAGKAVKVLP LSVDRAEDFA AVKSFMDVQQ PLEVYADQNF QAPSKYKISG MPGTLILDKQ
GRLVARLDGE TKWDTPEVQA LLDKLLAE
//
