(data stored in SCRATCH zone)

SWISSPROT: D3VJF1_XENNA

ID   D3VJF1_XENNA            Unreviewed;       131 AA.
AC   D3VJF1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 49.
DE   RecName: Full=Fumarate reductase subunit C {ECO:0000256|HAMAP-Rule:MF_00708, ECO:0000256|SAAS:SAAS00819766};
DE   AltName: Full=Fumarate reductase 15 kDa hydrophobic protein {ECO:0000256|HAMAP-Rule:MF_00708};
GN   Name=frdC {ECO:0000256|HAMAP-Rule:MF_00708,
GN   ECO:0000313|EMBL:CBJ88707.1};
GN   OrderedLocusNames=XNC1_0636 {ECO:0000313|EMBL:CBJ88707.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88707.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88707.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Seems to be involved in the anchoring of the catalytic
CC       components of the fumarate reductase complex to the cytoplasmic
CC       membrane. {ECO:0000256|HAMAP-Rule:MF_00708,
CC       ECO:0000256|SAAS:SAAS00819723}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two
CC       hydrophobic anchor proteins (FrdC and FrdD). {ECO:0000256|HAMAP-
CC       Rule:MF_00708, ECO:0000256|SAAS:SAAS00819749}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00708}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00708}.
CC   -!- SIMILARITY: Belongs to the FrdC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00708, ECO:0000256|SAAS:SAAS00819752}.
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DR   EMBL; FN667742; CBJ88707.1; -; Genomic_DNA.
DR   RefSeq; WP_013183378.1; NC_014228.1.
DR   STRING; 406817.XNC1_0636; -.
DR   EnsemblBacteria; CBJ88707; CBJ88707; XNC1_0636.
DR   KEGG; xne:XNC1_0636; -.
DR   eggNOG; ENOG4108WJH; Bacteria.
DR   eggNOG; COG3029; LUCA.
DR   HOGENOM; HOG000281484; -.
DR   KO; K00246; -.
DR   OMA; MTATWWQ; -.
DR   Proteomes; UP000008075; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00546; QFR_TypeD_subunitC; 1.
DR   Gene3D; 1.20.1300.10; -; 1.
DR   HAMAP; MF_00708; Fumarate_red_C; 1.
DR   InterPro; IPR003510; Fumarate_red_C.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   Pfam; PF02300; Fumarate_red_C; 1.
DR   PIRSF; PIRSF000180; FrdC; 1.
DR   ProDom; PD015900; Fumarate_red_C; 1.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VJF1.
DR   SWISS-2DPAGE; D3VJF1.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00708};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00708,
KW   ECO:0000256|SAAS:SAAS00832427};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00708,
KW   ECO:0000256|SAAS:SAAS00832430};
KW   Oxidoreductase {ECO:0000313|EMBL:CBJ88707.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00708,
KW   ECO:0000256|SAAS:SAAS00832426};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00708,
KW   ECO:0000256|SAAS:SAAS00832424}.
FT   TRANSMEM     21     48       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00708}.
FT   TRANSMEM     68     88       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00708}.
FT   TRANSMEM    109    130       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00708}.
SQ   SEQUENCE   131 AA;  14890 MW;  5E8B73FE66CE1445 CRC64;
     MTTKRKPYVR GMRPNWWHKL GFYRFYMLRE GTSVPAVWFS LLVLYGLFAL KNGPESWAGF
     VAFLQNPIVL LINIITLLAA LLHTKTWFEL APKALNIIVK NEKMAPGPVI KLLWAMTMIA
     TAAILGIALL F
//

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