ID G2I1U4_KOMMN Unreviewed; 262 AA.
AC G2I1U4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Outer membrane protein {ECO:0000313|EMBL:BAK84880.1};
GN OrderedLocusNames=GLX_24680 {ECO:0000313|EMBL:BAK84880.1};
OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS Kondo 51) (Gluconacetobacter medellinensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK84880.1, ECO:0000313|Proteomes:UP000009044};
RN [1] {ECO:0000313|Proteomes:UP000009044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC {ECO:0000313|Proteomes:UP000009044};
RX PubMed=22123756; DOI=10.1128/JB.06158-11;
RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT strain of Gluconacetobacter xylinus isolated from vinegar.";
RL J. Bacteriol. 193:6997-6998(2011).
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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; AP012159; BAK84880.1; -; Genomic_DNA.
DR RefSeq; WP_014106375.1; NC_016027.1.
DR AlphaFoldDB; G2I1U4; -.
DR STRING; 634177.GLX_24680; -.
DR KEGG; gxy:GLX_24680; -.
DR PATRIC; fig|634177.7.peg.2758; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_000288_47_4_5; -.
DR Proteomes; UP000009044; Chromosome.
DR CDD; cd03023; DsbA_Com1_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR041205; ScsC_N.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF5; THIOREDOXIN-LIKE_FOLD DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF18312; ScsC_N; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..262
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003431438"
FT DOMAIN 68..262
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 262 AA; 28066 MW; 35803AE4F3697676 CRC64;
MTFISPRRYR PRLLHALLAM GAVMVAMPDT GHAADPAESF TPAQRQEIVA IMRNALRTDP
TILSDAIAAL RSNANAAQQN AARGALESHR ADLLTPAASD AILGNPQGHT TVVEFYDPRC
PYCRKVLPDL DRLTREDKDL RIVEKVIPVL GQGSLITSQA LVAAFVQGGQ AAYFRMQAAV
MGDSASPTVE RMRTLATQSG LNATTLATDM NGAKVTAILQ ANMELARAIG LDGTPTFVFN
ARQIIPGAVG YDDLKKAIAQ SR
//
