ID S9RRV0_9RALS Unreviewed; 623 AA.
AC S9RRV0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:EPX94993.1};
GN ORFNames=C404_26320 {ECO:0000313|EMBL:EPX94993.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX94993.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX94993.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX94993.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(2014).
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:EPX94993.1}.
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DR EMBL; ASZV01000050; EPX94993.1; -; Genomic_DNA.
DR AlphaFoldDB; S9RRV0; -.
DR PATRIC; fig|1235457.3.peg.5237; -.
DR eggNOG; COG4232; Bacteria.
DR Proteomes; UP000015343; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; 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; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..623
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004568700"
FT TRANSMEM 209..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 484..618
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 623 AA; 65075 MW; A008767A7DA281BA CRC64;
MLLLAVLWFC VAGSGGVAHA AEEENLLPPE QAFRFAARQL DDRSIEVHFD IADGYHLFRE
RFVFAAQPAG VKLGTPEFPP GQVKFDEALG KQMEIYHGGV TIRVPVAVVP ADGEWLLTVT
SQGCADKGIC YPPMHSVYKV GGGLLGGLFD KHRSSRPMTS PVPPAMPILP SLGEGQIGPA
VPSAAPRNDD GDRVAHVLAG HQLGRIATVF FGLGLLMTLT PGVLAMVPIL SSIVVGEHVT
RGRALVVSLA YVLGTAVADA GVGVAAGLLG ERFSTGLLTP WALGAFTMLA VALALSMFGL
YELGRLPPMT ASSNRWSGGR IAVAAAAGVI SALVVVRSVP VPLSGTLTDA EQTGDAIGSG
GALFGMAIGM GAPLVLVGVA TGYLVPRAGH WLMVTKRFLG FLLLGEALWA VSPLLPPWAL
MAAWAMLLLI ASAFLGAFGS LGPEPRSLTR LGKGMGMVAA LAGAILLVGL ASGGRDLLQP
LSHLRAGLMA PASTAGPALV RFERIRSVAE LDARLVQAAA AGKPVLLDFY ADWCVSCKEM
ERLTFSDPRV QARLADVVLL QADVTRNSAD DRTLLKRFGL FGPPGIILYG ADGRESPVRV
IGFQSASLFL DSLAKAFGDD GKH
//
