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RNFD_SHEB8
ID   RNFD_SHEB8              Reviewed;         349 AA.
AC   A6WN15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00462};
DE   AltName: Full=Rnf electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462};
GN   Name=rnfD {ECO:0000255|HAMAP-Rule:MF_00462};
GN   OrderedLocusNames=Shew185_2062;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_00462}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00462};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00462}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00462}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00462}.
CC   -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00462}.
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DR   EMBL; CP000753; ABS08204.1; -; Genomic_DNA.
DR   RefSeq; WP_012089128.1; NC_009665.1.
DR   AlphaFoldDB; A6WN15; -.
DR   SMR; A6WN15; -.
DR   KEGG; sbm:Shew185_2062; -.
DR   HOGENOM; CLU_042020_0_0_6; -.
DR   OMA; GWQWINL; -.
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:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   HAMAP; MF_00462; RsxD_RnfD; 1.
DR   InterPro; IPR004338; NqrB/RnfD.
DR   InterPro; IPR011303; RnfD.
DR   PANTHER; PTHR30578; PTHR30578; 1.
DR   PANTHER; PTHR30578:SF0; PTHR30578:SF0; 1.
DR   Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR   TIGRFAMs; TIGR01946; rnfD; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW   Membrane; Phosphoprotein; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..349
FT                   /note="Ion-translocating oxidoreductase complex subunit D"
FT                   /id="PRO_1000013627"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        77..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   MOD_RES         185
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
SQ   SEQUENCE   349 AA;  37514 MW;  952F6DE3B60D21B6 CRC64;
     MAFKIASSPH VTRNLHTSTV MQRVILCLLP GLVVQCAFFG WGTLVQVLLA ILVALSCEAA
     VMKLRNRNIK ASLSDNSAML TAILIGVAIP PLAPWWMIVM GTAFAIVIVK HLYGGLGHNL
     FNPAMAAYVL LLVSFPVQMT TWIAPSTVAL HSPSLVESLQ LIFNIGAHVN MEQFRLGIDG
     MTMATPLDTL KTDLSMGLTT TESLTKAIFD GSTGVGWFWV NLAYLAGGLV LLKLKAIRWH
     ISTGVLLGLF VASSIGFLLS PDTQASPLMH LFSGATMLAA FFIATDPVTA ATSPRGRIIF
     GALIGVLVYI IRTKGGYPDA FAFAVLLANL CAPFIDYYVR PRTYGHSTS
 
 
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