ID A0A011QGU7_9PROT Unreviewed; 608 AA. AC A0A011QGU7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 17-FEB-2016, entry version 9. DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399}; DE EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399}; DE AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399}; DE Flags: Precursor; GN Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399, GN ECO:0000313|EMBL:EXI88517.1}; GN ORFNames=AW11_02137 {ECO:0000313|EMBL:EXI88517.1}; OS Candidatus Accumulibacter sp. BA-93. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454004 {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141}; RN [1] {ECO:0000313|EMBL:EXI88517.1, ECO:0000313|Proteomes:UP000022141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required to facilitate the formation of correct CC disulfide bonds in some periplasmic proteins and for the assembly CC of the periplasmic c-type cytochromes. Acts by transferring CC electrons from cytoplasmic thioredoxin to the periplasm. This CC transfer involves a cascade of disulfide bond formation and CC reduction steps. {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein CC disulfide + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00399}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000256|HAMAP- CC Rule:MF_00399}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXI88517.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JEMY01000026; EXI88517.1; -; Genomic_DNA. DR Proteomes; UP000022141; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.40.1250; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00399; DbsD; 1. DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom. DR InterPro; IPR028250; DsbDN. DR InterPro; IPR022910; Thiol_diS_interchange_DbsD. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1. DR Pfam; PF11412; DsbC; 1. DR Pfam; PF02683; DsbD; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF74863; SSF74863; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00399}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00512526}; KW Complete proteome {ECO:0000313|Proteomes:UP000022141}; KW Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00399}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464083}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00399}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000313|EMBL:EXI88517.1}; KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00399}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464121}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464105}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00399}. FT SIGNAL 1 37 {ECO:0000256|HAMAP-Rule:MF_00399}. FT CHAIN 38 608 Thiol:disulfide interchange protein DsbD. FT {ECO:0000256|HAMAP-Rule:MF_00399}. FT /FTId=PRO_5004993609. FT TRANSMEM 185 205 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 242 262 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 273 293 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 327 347 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 354 374 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 388 408 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 411 431 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT TRANSMEM 451 471 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT DOMAIN 467 608 Thioredoxin. {ECO:0000259|PROSITE: FT PS51352}. FT DISULFID 138 144 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT DISULFID 210 335 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00399}. FT DISULFID 524 527 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00399}. SQ SEQUENCE 608 AA; 64989 MW; 497E8D24EF2DC87E CRC64; MTWLFVLPHS VRRFFQRSSL LPFLLPVLML LTWPAQGEEF LDPAVAFKPT AHAVDGQTIE VRFEIAKGYY LYRDKFRFTA EPASVQLGTP ILSPGKVKED PNFGKVEVYY KQALIRIPVE RNSSGPLPLT LKITSQGCAD AGICYPPQRQ TLALELPDPA TTPSAGATTP GKDFGDDESG RIAQLFGNAS FWLLVASFFG FGLLLSLTPC CFPMIPILSS IIVGSGRDGH GVSHARGFSL SLAYVLGMAI TYAAAGVAAG LTGTLLTAAL QNAWVLGAFA LVFVALSLSM FGFYELQLPT FLQSKVSEEA SHLRGGSLPG VAAMGVLSAI IVGPCVAAPL AGALLYIGRS GDAVLGGAAL FAMGLGMGAP LLAVGLSAGT LLPRSGPWME AVKKSFGVLL LATAVWLLSP VVPVVAQMIA WALLLIVPAI YMHALDPLPP HARGWQRFWK GIGIFMLIGG AAMLLGALAG SRDPLQPLSA LRSSAAEVEV KQLPFTRVRT LAELERRIKS AGQPVMIDFY ADWCVSCKEM ERFTFADARV RAKLAGWTLL QADVTANSDE DKALLQRFNL YGPPGIIFFD AQGREIDGVR VVGFMSADEF LGLLARLG //