ID A0A0Q5Q4U3_9FLAO Unreviewed; 391 AA.
AC A0A0Q5Q4U3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Disulfide isomerase {ECO:0000313|EMBL:KQR92575.1};
GN ORFNames=ASG01_11760 {ECO:0000313|EMBL:KQR92575.1};
OS Chryseobacterium sp. Leaf180.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR92575.1, ECO:0000313|Proteomes:UP000051405};
RN [1] {ECO:0000313|EMBL:KQR92575.1, ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|EMBL:KQR92575.1,
RC ECO:0000313|Proteomes:UP000051405};
RX PubMed=26633631; DOI=10.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR92575.1}.
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DR EMBL; LMPJ01000010; KQR92575.1; -; Genomic_DNA.
DR RefSeq; WP_055863993.1; NZ_LMPJ01000010.1.
DR AlphaFoldDB; A0A0Q5Q4U3; -.
DR STRING; 1736289.ASG01_11760; -.
DR OrthoDB; 120730at2; -.
DR Proteomes; UP000051405; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KQR92575.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051405};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..391
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006259471"
FT DOMAIN 3..134
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 391 AA; 44852 MW; 089DFDC0126E2D85 CRC64;
MTKIFSVLLL SFAFICKAQG EMKFEEIPFK ELIAKAKKEN KLVFIDAYAS WCGPCKMMER
NIFPKKTVGD VYNKSFVNAR IDMEKGEGRE IAQKYGVRSY PTYLFLNGDG ELISQNFGYM
EESAFIAMAN DLNSPDNKKG SLKDRFAAGE NDSEFLINIM RLNSSSDFDF AKKASERYFD
NKKKTDEFTK DDVGLLLYFL KSPEDKNYRV FTERKADIIK FLPEETYKEF NDQIVLARIL
TESIDDKSKK INDAYYFHKA VPLVGKEAAE TKLLQTKLAF YEQNGNFAEY EKAALAYYRD
SEKFDKNELL KAAWVFSDNV KNHASLKKAA EWAEKSVMTG ETAENTYILA KIYSLLGNKE
LAKNFAEMSR NIAKQSGKDA SLAEELLQKF K
//