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 01-MAY-2013, entry version 81.
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).
CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC histidine/cysteine.
CC -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (Potential).
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 (By similarity).
CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
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DR EMBL; AE013218; AAM68090.1; -; Genomic_DNA.
DR RefSeq; NP_660879.1; 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; ITHKDLT; -.
DR ProtClustDB; CLSK2459983; -.
DR BioCyc; BAPH198804:GHMG-592-MONOMER; -.
DR GO; GO:0016021; C:integral to 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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_2.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
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; SSF55804; PTrfase/Anion_transptr; 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; (Potential).
FT TRANSMEM 47 67 Helical; (Potential).
FT TRANSMEM 94 114 Helical; (Potential).
FT TRANSMEM 134 154 Helical; (Potential).
FT TRANSMEM 161 181 Helical; (Potential).
FT TRANSMEM 214 234 Helical; (Potential).
FT TRANSMEM 245 265 Helical; (Potential).
FT TRANSMEM 267 287 Helical; (Potential).
FT TRANSMEM 291 311 Helical; (Potential).
FT TRANSMEM 316 336 Helical; (Potential).
FT DOMAIN 12 340 PTS EIIC type-2.
FT DOMAIN 380 472 PTS EIIB type-2.
FT DOMAIN 503 645 PTS EIIA type-2.
FT ACT_SITE 386 386 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT ACT_SITE 563 563 Tele-phosphohistidine intermediate; for
FT EIIA activity (By similarity).
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
//
