ID A0A074MB14_ERYLO Unreviewed; 702 AA.
AC A0A074MB14;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:KEO92011.1};
GN ORFNames=EH31_04890 {ECO:0000313|EMBL:KEO92011.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO92011.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO92011.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO92011.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-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:KEO92011.1}.
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DR EMBL; JMIW01000001; KEO92011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074MB14; -.
DR STRING; 1044.EH31_04890; -.
DR eggNOG; COG4232; Bacteria.
DR eggNOG; COG4233; Bacteria.
DR Proteomes; UP000027647; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..702
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001696934"
FT TRANSMEM 309..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 573..702
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 702 AA; 74443 MW; 40CE439017A1324B CRC64;
MFAASPFAIH AWFKALLLAI AALLAFPTAL WAQEVDAERE RALTRIERAG DDRISVDLFA
DGAPRAGETW MLALRFTPSA PEWHGYWANP GDAGLGMQLE LDLPEGWQAG EALYPVPKRL
LIAELMNHIY EGEYAVLVPV KVPADAVIEG IPEVTGIVEY LACTDEICVP QGAAFSAGQA
GVLGGDFARW RAEVAPMLDA SATFTVTDGA LRLGIPLPGS VELSDPHVFI ANTQLVDYAP
FQNFWRDGDR LVVEIPLSEF GTGEAERVEG ILAFDEQTGV RFVAARGEVA VGGERLVVMN
SAEGAAPPLW TLILGALVGG LILNIMPCVF PILSLKAISL ARAGGGEAEA RAEGLAYTAG
VVLACVALGG IMLALRAAGE QVGWAFQLQS PGVVIVLLVL ATVITLNFAG IFELPSVDTG
GGHGRSAFAT GLLAAVAATP CTGPFMAAAL GAALLLPTPL ALLLFAMLGL GLALPFLLIG
FVPPLRKMLP KPGAWMETFR RAMAIPMGLT ALALIWLTVQ LGGRGFGGFA LVMLFGIVLA
LFIVGRLQQA GKMAWPAFGL VVAPFLIFGA FALPYAYAPP SRDLSASLLE PQAFSREALA
EARNSGQPVF VWFTADWCVT CKVNESVAIE REATAQAFAD AGVVAIVGDW TVRDEEITQF
LTEQGAAGVP LYLWYEPGVA EPEQLPQVLT PEMLSERAQK DR
//
