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Database: UniProt
Entry: A0A0H2KP28_9MICO
LinkDB: A0A0H2KP28_9MICO
Original site: A0A0H2KP28_9MICO 
ID   A0A0H2KP28_9MICO        Unreviewed;       668 AA.
AC   A0A0H2KP28;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:KLN35270.1};
GN   ORFNames=FB00_07535 {ECO:0000313|EMBL:KLN35270.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35270.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN35270.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN35270.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KLN35270.1}.
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DR   EMBL; JNBQ01000005; KLN35270.1; -; Genomic_DNA.
DR   RefSeq; WP_047232261.1; NZ_JNBQ01000005.1.
DR   AlphaFoldDB; A0A0H2KP28; -.
DR   STRING; 264251.FB00_07535; -.
DR   PATRIC; fig|264251.5.peg.1533; -.
DR   Proteomes; UP000035265; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-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; IPR041017; Thioredoxin_10.
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   Pfam; PF17991; Thioredoxin_10; 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:UP000035265};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          363..513
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          70..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  70366 MW;  91FC8850602BBCEF CRC64;
     METLIVIGLL GGLITGVSPC ILPMLPVIFF AGGVQGARTG EPPSGTSEPG TGGVSPRLFA
     GVPDAVRVGG RPAAGLRGRG GPGGAQEAAG TREVTARPTR GGTLALDLST GDAAEPATPV
     DGGPGRRASR RAARRSWRPY LVIAGLVLSF SVFTLLGSLL LTALGLPQDL LRWAGIVLLV
     AIGVGMIVPR VEEVLERPFR RIAALGARRG AARQDRGAFV LGLGLGVLYV PCAGPVLAAI
     TVAGATGNIG PGTVALTVSF AVGAAVPLLV FALAGRRVAE RVRGFQRHTR GIRVTGGVVM
     IALAGALALN LPAALQRALP DYTGALQQRV DENDAVREAL DLGGLVTDEN RELSNCSNGA
     PVLEDCGTAP ELRGIDTWLN TPGGEALTLE GLRGKVVLVD FWTYSCINCQ RAIPHVNAWY
     DRYRDVGAGF EVVGVHTPEF AFERETRNVV AGAQDLGVTY PVAQDNAYAT WTAYRNRYWP
     AQYLVDADGT VRHIRFGEGG YEDTERLVRE LLEDANPGVE LPAPTAVGDT TPQDETTPET
     YFSIKRVVNY AGEPRYAAGQ QDFTLADDQR QDTFSLGGTW DVDFQGATAV SDDARVRLAY
     RSTDVFTVLG GEGTVTARVT KDGRTTTREI DVSGSPTLYP VLEGDGPTEG LVELDVPPGV
     QVFTATFG
//
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