ID   A0A327QC15_9BACT        Unreviewed;       458 AA.
AC   A0A327QC15;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Thiol-disulfide isomerase/thioredoxin {ECO:0000313|EMBL:RAJ01515.1};
GN   ORFNames=LX64_03730 {ECO:0000313|EMBL:RAJ01515.1};
OS   Chitinophaga skermanii.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=331697 {ECO:0000313|EMBL:RAJ01515.1, ECO:0000313|Proteomes:UP000249547};
RN   [1] {ECO:0000313|EMBL:RAJ01515.1, ECO:0000313|Proteomes:UP000249547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23857 {ECO:0000313|EMBL:RAJ01515.1,
RC   ECO:0000313|Proteomes:UP000249547};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) 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:RAJ01515.1}.
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DR   EMBL; QLLL01000007; RAJ01515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327QC15; -.
DR   OrthoDB; 1095575at2; -.
DR   Proteomes; UP000249547; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; 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   Isomerase {ECO:0000313|EMBL:RAJ01515.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249547};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..458
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016283865"
FT   DOMAIN          316..457
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          439..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  51958 MW;  9AE47DA5E352C4D3 CRC64;
     MKKLRLMLVA LAAWGIVPVC AAPVVGPTVI QGQVDNEKIN SITLFKTEDG HRVKVATVNV
     EDKQFAFALT KVTEGYYYIG DAGEKDLARV YLKNNDQLSI VLHDDGAELK AGSVENKKLY
     EWEKAINPLA RPAHQFWKGN YTYDEVFPVL EALLPKVTTF KKGINTPNKN FNELLKYTVD
     ADIEYAAMHL LYTPRSKHPL EEDKPAYYKT IAQDVKFTNP NIMKIGYAKD YVSLYVMHVF
     TTKMKASKEK PTMPTLAENV KLFGLDDVKA MFILNSITRY KTYEELATAV EPVKGLLKTK
     NQIDAYNEVE RSLRSFKKGT AGYNFKYPDT NGKEVAFSDL KGKVVVVDVW ATWCGPCKKE
     IPFLKELEKE MEGKDVTFVG VSVDEAKDKQ KWIDFVKKEE LAGIQIFATG WSEITKFYNI
     TGIPRFMVFD KKGNVVSIDS PRPSSPDLKK MIEEELKK
//