GenomeNet

Database: UniProt
Entry: C6JIS8_FUSVA
LinkDB: C6JIS8_FUSVA
Original site: C6JIS8_FUSVA 
ID   C6JIS8_FUSVA            Unreviewed;       315 AA.
AC   C6JIS8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 2.
DT   27-SEP-2017, entry version 32.
DE   RecName: Full=2-keto-3-deoxygluconate permease {ECO:0000256|HAMAP-Rule:MF_00070};
DE            Short=KDG permease {ECO:0000256|HAMAP-Rule:MF_00070};
GN   Name=kdgT {ECO:0000256|HAMAP-Rule:MF_00070};
GN   ORFNames=FVAG_01229 {ECO:0000313|EMBL:EES64546.2};
OS   Fusobacterium varium ATCC 27725.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=469618 {ECO:0000313|EMBL:EES64546.2, ECO:0000313|Proteomes:UP000004505};
RN   [1] {ECO:0000313|EMBL:EES64546.2, ECO:0000313|Proteomes:UP000004505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES64546.2,
RC   ECO:0000313|Proteomes:UP000004505};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA   Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium varium ATCC 27725.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 2-keto-3-deoxygluconate permease transports the
CC       degraded pectin products into the bacterial cell, where they serve
CC       as carbon and energy sources. This is a hydrogen coupled transport
CC       system. {ECO:0000256|HAMAP-Rule:MF_00070}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00070}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00070}.
CC   -!- SIMILARITY: Belongs to the KdgT transporter family.
CC       {ECO:0000256|HAMAP-Rule:MF_00070}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00070}.
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:EES64546.2}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; ACIE02000013; EES64546.2; -; Genomic_DNA.
DR   RefSeq; WP_005948761.1; NZ_GL987996.1.
DR   STRING; 469618.FVAG_01229; -.
DR   EnsemblBacteria; EES64546; EES64546; FVAG_01229.
DR   eggNOG; ENOG4105CAX; Bacteria.
DR   eggNOG; ENOG410XNUJ; LUCA.
DR   OrthoDB; POG091H07SX; -.
DR   Proteomes; UP000004505; 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:0015649; F:2-keto-3-deoxygluconate:proton symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005351; F:sugar:proton symporter activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00070; KdgT; 1.
DR   InterPro; IPR004684; 2keto-3dGluconate_permease.
DR   Pfam; PF03812; KdgT; 1.
DR   ProDom; PD024513; 2keto-3dGluconate_permease; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004505};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004505};
KW   Sugar transport {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Symport {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00070}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM     45     63       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM     75     95       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    101    123       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    159    181       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    193    212       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    218    237       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    249    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    280    303       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
SQ   SEQUENCE   315 AA;  32125 MW;  ECDDAFADCE234442 CRC64;
     MKIKKSIERI PGGMMVVPLI IGAVMNTFCP QILDIGSFTT NLARGAMPIL AVFLVCMGAE
     INLKAAPQVI KKGSVITISK FVIGAVIGIL VSKFMGSEGL FGLSALAIIA AMTNSNGGLY
     AALTGEFGNA TDTGAIAIVS LNDGPFLTMI ALGSAGVAAI PFSILIGAVI PILLGALLGN
     LDEDMKEFLS KAGGVMIPFF AFGLGCGINL SMLIKAGIPG LVLGLMTVIV GGIFNILSDK
     LTGGSGIAGA AISSTSGNAV ATPLAIAAMD PRLLETAKIA TAQVAASTIL TAFLVPVLTT
     YVYKYNQKKK ESIKI
//
DBGET integrated database retrieval system