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Database: UniProt
Entry: Q8K911
LinkDB: Q8K911
Original site: Q8K911 
ID   PTM3C_BUCAP             Reviewed;         649 AA.
AC   Q8K911;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   29-OCT-2014, entry version 93.
DE   RecName: Full=PTS system mannitol-specific EIICBA component;
DE   AltName: Full=EIICBA-Mtl;
DE            Short=EII-Mtl;
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component;
DE     AltName: Full=PTS system mannitol-specific EIIC component;
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system mannitol-specific EIIB component;
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system, mannitol-specific EIIA component;
GN   Name=mtlA; OrderedLocusNames=BUsg_552;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       -transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. This system is involved in mannitol transport (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- PTM: An intramolecular phosphotransfer takes places between His-
CC       563 and Cys-386. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
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DR   EMBL; AE013218; AAM68090.1; -; Genomic_DNA.
DR   RefSeq; NP_660879.1; NC_004061.1.
DR   RefSeq; WP_011054056.1; NC_004061.1.
DR   ProteinModelPortal; Q8K911; -.
DR   SMR; Q8K911; 379-467, 503-643.
DR   STRING; 198804.BUsg552; -.
DR   EnsemblBacteria; AAM68090; AAM68090; BUsg_552.
DR   GeneID; 1005638; -.
DR   KEGG; bas:BUsg552; -.
DR   PATRIC; 21247984; VBIBucAph100086_0584.
DR   eggNOG; COG4668; -.
DR   KO; K02798; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; PGMGVLM; -.
DR   OrthoDB; EOG6FBWWQ; -.
DR   BioCyc; BAPH198804:GHMG-583-MONOMER; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10370; -; 1.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Kinase; Membrane;
KW   Phosphotransferase system; Sugar transport; Transferase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    649       PTS system mannitol-specific EIICBA
FT                                component.
FT                                /FTId=PRO_0000186612.
FT   TRANSMEM     20     40       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM     47     67       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM     94    114       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    134    154       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    161    181       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    214    234       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    245    265       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    267    287       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    291    311       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    316    336       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN       12    340       PTS EIIC type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN      380    472       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   DOMAIN      503    645       PTS EIIA type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00417}.
FT   ACT_SITE    386    386       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000250}.
FT   ACT_SITE    563    563       Tele-phosphohistidine intermediate; for
FT                                EIIA activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00417}.
SQ   SEQUENCE   649 AA;  72358 MW;  B365CE4719C986C0 CRC64;
     MFRLITLKIQ NFGQFLSNMI MPNISIFITW GIMNSLFLSL DWQYNKIFAQ LISPIIFYLL
     PILIGYTGGS LIAGQRGGLL GSITTIGMIT STDMPMFLGG MVAGPLGGWI IKGFDQIIKN
     RIKSGFEMLV NNFSIAIIGI FLTIFSFFFI GPFIEGVSKF LGCLIKIIID FNLLPLIAFI
     IEPAKVFFLN NAINHGIFSP LGIQEISENK SSLFFLIESN PGPGLGILIA CFFFGKEKSY
     KSSGTAAIVQ FLGGIHEIYF SYVLIKPILM ISLILGSMTS IFMLVFFKGG LIAAVSPGSI
     LSILAMTKKG LYFANLISIF SSFLISFLSA MLFFKINLGQ KIKNDKSSIQ LFKNNLFPIK
     KIGDEKYDFI KKIKNFQKIK NIIIACDAGM GSSAMGASIL RKKIKSNNLT HIYVSNIAIN
     LLPKNADLVI THEKLTYLAK KRAPDAQHIS LTNFLDSNFY TSLVKQLDLN KDFFKKNNIQ
     DKKDRITQIN IDSHKEIQSK CFFQISDKNI FLNQYAENKK EAIKIVGKHL VAQGYVKKDY
     IDAMLDREKI ASTWLGESVA LPHGTIKSKD SILKTGVIFC QFPKGVHFGE TIDDIAYLVI
     GIAAKNNEHI MVVSNITNAL DDKDVISKLS KTKSVKEVLS YLNVNVKKN
//
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