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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   07-JUN-2017, entry version 110.
DE   RecName: Full=PTS system mannitol-specific EIICBA component {ECO:0000250|UniProtKB:P00550};
DE   AltName: Full=EIICBA-Mtl {ECO:0000250|UniProtKB:P00550};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P00550};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P00550};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P00550};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P00550};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P00550};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P00550};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550};
DE     AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P00550};
GN   Name=mtlA; OrderedLocusNames=BUsg_552;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; 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 D-mannitol transport.
CC       {ECO:0000250|UniProtKB:P00550}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
CC       mannitol(Side 1) = [protein]-L-histidine + D-mannitol 1-
CC       phosphate(Side 2). {ECO:0000250|UniProtKB:P00550}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00550}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P00550, ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00550, ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
CC   -!- INDUCTION: Induced by mannitol. Repressed by MltR.
CC       {ECO:0000250|UniProtKB:P00550}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-
CC       EIIA on a cysteinyl residue. Then, it transfers the phosphoryl
CC       group to the sugar substrate concomitantly with the sugar uptake
CC       processed by the PTS EIIC type-2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00422}.
CC   -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-
CC       HPr on a histidyl residue. Then, it transfers the phosphoryl group
CC       to the PTS EIIB type-2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00417}.
CC   -!- PTM: An intramolecular phosphotransfer takes places between His-
CC       563 and Cys-386. {ECO:0000250|UniProtKB:P00550}.
DR   EMBL; AE013218; AAM68090.1; -; Genomic_DNA.
DR   RefSeq; WP_011054056.1; NC_004061.1.
DR   ProteinModelPortal; Q8K911; -.
DR   SMR; Q8K911; -.
DR   STRING; 198804.BUsg552; -.
DR   PRIDE; Q8K911; -.
DR   EnsemblBacteria; AAM68090; AAM68090; BUsg_552.
DR   KEGG; bas:BUsg_552; -.
DR   eggNOG; ENOG4105CTS; Bacteria.
DR   eggNOG; COG2213; LUCA.
DR   eggNOG; COG4668; LUCA.
DR   KO; K02798; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; SIIHFFG; -.
DR   OrthoDB; POG091H0GYI; -.
DR   Proteomes; UP000000416; 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: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   CDD; cd05567; PTS_IIB_mannitol; 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 inner membrane; Cell membrane; Complete proteome; Kinase;
KW   Membrane; Phosphoprotein; Phosphotransferase system; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    649       PTS system mannitol-specific EIICBA
FT                                component.
FT                                /FTId=PRO_0000186612.
FT   TRANSMEM     24     45       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     50     70       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    134    155       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    165    185       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    273    292       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    313    334       Helical. {ECO:0000250|UniProtKB:P00550}.
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|UniProtKB:P00550}.
FT   ACT_SITE    563    563       Tele-phosphohistidine intermediate; for
FT                                EIIA activity.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000255|PROSITE-ProRule:PRU00417}.
FT   SITE        547    547       Stabilizes the transition state in the
FT                                phosphoryl transfer from HPr to EIIA.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   MOD_RES     386    386       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000255|PROSITE-ProRule:PRU00422}.
FT   MOD_RES     563    563       Phosphohistidine; by HPr.
FT                                {ECO:0000250|UniProtKB:P00550}.
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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