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Database: UniProt
Entry: KDGT_BACSU
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Original site: KDGT_BACSU 
ID   KDGT_BACSU              Reviewed;         330 AA.
AC   P50847;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   07-JUN-2017, entry version 104.
DE   RecName: Full=2-keto-3-deoxygluconate permease;
DE            Short=KDG permease;
GN   Name=kdgT; OrderedLocusNames=BSU22090;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / VKM B-501;
RX   PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between
RT   the serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=9846747; DOI=10.1099/00221287-144-11-3111;
RA   Pujic P., Dervyn R., Sorokin A., Ehrlich S.D.;
RT   "The kdgRKAT operon of Bacillus subtilis: detection of the transcript
RT   and regulation by the kdgR and ccpA genes.";
RL   Microbiology 144:3111-3118(1998).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Induced by galacturonate and negatively regulated by
CC       the KdgR repressor. Is subject to catabolite repression by glucose
CC       involving the ccpA gene. {ECO:0000269|PubMed:9846747}.
CC   -!- SIMILARITY: Belongs to the KdgT transporter family. {ECO:0000305}.
DR   EMBL; L47838; AAB38481.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14126.1; -; Genomic_DNA.
DR   PIR; C69648; C69648.
DR   RefSeq; NP_390091.1; NC_000964.3.
DR   RefSeq; WP_003230734.1; NZ_JNCM01000036.1.
DR   ProteinModelPortal; P50847; -.
DR   STRING; 224308.Bsubs1_010100012161; -.
DR   TCDB; 2.A.10.1.3; the 2-keto-3-deoxygluconate transporter (kdgt) family.
DR   PaxDb; P50847; -.
DR   EnsemblBacteria; CAB14126; CAB14126; BSU22090.
DR   GeneID; 939065; -.
DR   KEGG; bsu:BSU22090; -.
DR   PATRIC; fig|224308.179.peg.2413; -.
DR   eggNOG; ENOG4105CAX; Bacteria.
DR   eggNOG; ENOG410XNUJ; LUCA.
DR   HOGENOM; HOG000221851; -.
DR   InParanoid; P50847; -.
DR   KO; K02526; -.
DR   OMA; ESGPFMT; -.
DR   PhylomeDB; P50847; -.
DR   BioCyc; BSUB:BSU22090-MONOMER; -.
DR   Proteomes; UP000001570; 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:0015649; F:2-keto-3-deoxygluconate:proton symporter activity; IEA:InterPro.
DR   HAMAP; MF_00070; KdgT; 1.
DR   InterPro; IPR004684; 2keto-3dGluconate_permease.
DR   InterPro; IPR018395; 2keto-3dGluconate_permease_sub.
DR   Pfam; PF03812; KdgT; 1.
DR   ProDom; PD024513; 2keto-3dGluconate_permease; 1.
DR   TIGRFAMs; TIGR00793; kdgT; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Membrane; Reference proteome;
KW   Sugar transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    330       2-keto-3-deoxygluconate permease.
FT                                /FTId=PRO_0000209674.
FT   TRANSMEM     10     30       Helical. {ECO:0000255}.
FT   TRANSMEM     42     62       Helical. {ECO:0000255}.
FT   TRANSMEM     77     97       Helical. {ECO:0000255}.
FT   TRANSMEM    100    120       Helical. {ECO:0000255}.
FT   TRANSMEM    140    160       Helical. {ECO:0000255}.
FT   TRANSMEM    164    184       Helical. {ECO:0000255}.
FT   TRANSMEM    200    220       Helical. {ECO:0000255}.
FT   TRANSMEM    224    244       Helical. {ECO:0000255}.
FT   TRANSMEM    254    274       Helical. {ECO:0000255}.
FT   TRANSMEM    289    309       Helical. {ECO:0000255}.
SQ   SEQUENCE   330 AA;  34319 MW;  6273AF3326BD99B6 CRC64;
     MKIKATIERV PGGMMIIPLF LGAALNTFAP GTAEFFGGFT GALITGTLPI LGVFIFCVGA
     TIDFRSSGYI ARKGITLLLG KIGFAALLGV IAAQFIPDDG IQSGFFAGLS VLAIVAVMNE
     TNGGLYLALM NHMGRKEDAG AFAFISTESG PFMTMVTFGV TGLAAFPWET LAATVIPFLL
     GCILGNLDHD LRDLFSKVVP AIIPFFAFSL GNTLNFGMLI QSGLLGIFIG VSVVILSGSS
     LFLLDRFIAR GDGVAGVAAS STAGAAVAVP YALAEANASF APVAESATAI IATSVIVTSL
     LTPLATVWVD KKIKQKKRRT PPPKNQMTIN
//
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