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Database: UniProt
Entry: A0A1H2FPE2_9BACT
LinkDB: A0A1H2FPE2_9BACT
Original site: A0A1H2FPE2_9BACT 
ID   A0A1H2FPE2_9BACT        Unreviewed;       700 AA.
AC   A0A1H2FPE2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:SDU09165.1};
GN   ORFNames=SAMN05444156_1907 {ECO:0000313|EMBL:SDU09165.1};
OS   Verrucomicrobium sp. GAS474.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; Verrucomicrobium.
OX   NCBI_TaxID=1882831 {ECO:0000313|EMBL:SDU09165.1, ECO:0000313|Proteomes:UP000198591};
RN   [1] {ECO:0000313|EMBL:SDU09165.1, ECO:0000313|Proteomes:UP000198591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS474 {ECO:0000313|EMBL:SDU09165.1,
RC   ECO:0000313|Proteomes:UP000198591};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; LT629781; SDU09165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2FPE2; -.
DR   STRING; 1882831.SAMN05444156_1907; -.
DR   OrthoDB; 9811036at2; -.
DR   Proteomes; UP000198591; Chromosome i.
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; IPR017937; Thioredoxin_CS.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000198591};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..700
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009274116"
FT   TRANSMEM        293..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        450..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        494..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        517..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          565..698
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   700 AA;  74252 MW;  352F0360143DBE17 CRC64;
     MHRPGLSLAL SLSLFLGLLA PLRADAPPET PHVQASLYLQ SWLYELPRPA EGEGVRADLS
     FHIEKGWHLY WRNPGDAGRA VKVLWHLPDG WTAEPLQWPV PKIYTLGTLT DYGYEGDLVL
     TAVLRPPALE TRKPKLNPAQ VSAELVWLVC SPEACLPGHT LLRPSPEPAG TKIYHDDSEV
     FPKPLPKGEA TLREAGAYLQ LSLSDADGLP SSGPLRFIPY ARGLIANGER QFAVRSAQGI
     ELRVKKAEGA DALPETVEGL LLAVDAGRGW EIKARVLPPL PVAPPSSGSG TGFPFAALGL
     AFLGGLLLNL MPCVLPVLSL KVLALVSMPR REGLRHGLAY TAGVVLSFLA LAGLLLALRA
     AGGRFGWGFQ LQSPAFVVLI AALFWAITLN LLGLFEIGEG LAARGGAVLE GRKKSVIAPF
     LGGLLAVIVA TPCTAPFMGT ALGVAFSQSA GVALLIFAAL GLGLAAPYLA LAANPAWLRF
     VPKSGGWMVW FRRLLALPMA VTVVWLVWVF HRETGGGAVL LLALGAVLCA AALFGKWEGK
     TMVSRLAVHT AALLLAGAAI SAAMVYHGVP KPASAAADSA QGEGDWIPYT NERLEAAREA
     GKPVFVDFTA DWCLPCQVNK QVLDAPEVAA RFREKGVVRL IADWTRNDPE VTAALAAAGR
     PSVPLSLLYG SNPALPPKIL PSLLTKRAVL DALDVLDSLK
//
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