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Database: UniProt
Entry: P69826
LinkDB: P69826
Original site: P69826 
ID   PTMCB_ECOLI             Reviewed;         462 AA.
AC   P69826; P32059; Q2M9R0;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-SEP-2014, entry version 79.
DE   RecName: Full=PTS system mannitol-specific cryptic EIICB component;
DE   AltName: Full=EIICB-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;
GN   Name=cmtA; OrderedLocusNames=b2933, JW2900;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-446.
RC   STRAIN=K12;
RX   PubMed=8353127; DOI=10.1016/0304-4165(93)90103-F;
RA   Sprenger G.A.;
RT   "Two open reading frames adjacent to the Escherichia coli K-12
RT   transketolase (tkt) gene show high similarity to the mannitol
RT   phosphotransferase system enzymes from Escherichia coli and various
RT   Gram-positive bacteria.";
RL   Biochim. Biophys. Acta 1158:103-106(1993).
RN   [2]
RP   PRESENCE OF VECTOR SEQUENCE CONTAMINATION IN SEQUENCE DESCRIBED IN
RP   PUBMED:8353127.
RA   Rudd K.E.;
RL   Unpublished observations (JUN-1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
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 EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
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   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA51229.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the C-terminus;
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DR   EMBL; X72677; CAA51229.1; ALT_TERM; Genomic_DNA.
DR   EMBL; U28377; AAA69100.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75970.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76996.1; -; Genomic_DNA.
DR   PIR; D65078; S36123.
DR   RefSeq; NP_417408.1; NC_000913.3.
DR   RefSeq; YP_491132.1; NC_007779.1.
DR   ProteinModelPortal; P69826; -.
DR   SMR; P69826; 368-462.
DR   IntAct; P69826; 3.
DR   STRING; 511145.b2933; -.
DR   EnsemblBacteria; AAC75970; AAC75970; b2933.
DR   EnsemblBacteria; BAE76996; BAE76996; BAE76996.
DR   GeneID; 12933074; -.
DR   GeneID; 945256; -.
DR   KEGG; ecj:Y75_p2863; -.
DR   KEGG; eco:b2933; -.
DR   PATRIC; 32121278; VBIEscCol129921_3027.
DR   EchoBASE; EB1740; -.
DR   EcoGene; EG11792; cmtA.
DR   eggNOG; COG2213; -.
DR   HOGENOM; HOG000252814; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; GMESEWR; -.
DR   OrthoDB; EOG6FBWWQ; -.
DR   PhylomeDB; P69826; -.
DR   BioCyc; EcoCyc:CMTA-MONOMER; -.
DR   BioCyc; ECOL316407:JW2900-MONOMER; -.
DR   BioCyc; MetaCyc:CMTA-MONOMER; -.
DR   PRO; PR:P69826; -.
DR   Genevestigator; P69826; -.
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:0015575; F:mannitol transmembrane transporter activity; IGI:EcoCyc.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015797; P:mannitol transport; IGI:EcoCyc.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10370; -; 1.
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   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00851; mtlA; 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; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    462       PTS system mannitol-specific cryptic
FT                                EIICB component.
FT                                /FTId=PRO_0000186679.
FT   TOPO_DOM      1     25       Cytoplasmic (Potential).
FT   TRANSMEM     26     45       Helical; (Probable).
FT   TOPO_DOM     46     51       Periplasmic (Potential).
FT   TRANSMEM     52     70       Helical; (Probable).
FT   TOPO_DOM     71    135       Cytoplasmic (Potential).
FT   TRANSMEM    136    155       Helical; (Probable).
FT   TOPO_DOM    156    166       Periplasmic (Potential).
FT   TRANSMEM    167    185       Helical; (Probable).
FT   TOPO_DOM    186    273       Cytoplasmic (Potential).
FT   TRANSMEM    274    294       Helical; (Probable).
FT   TOPO_DOM    295    316       Periplasmic (Potential).
FT   TRANSMEM    317    336       Helical; (Probable).
FT   TOPO_DOM    337    462       Cytoplasmic (Potential).
FT   DOMAIN       13    344       PTS EIIC type-2.
FT   DOMAIN      371    461       PTS EIIB type-2.
FT   ACT_SITE    377    377       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
FT   CONFLICT    274    275       MI -> IEF (in Ref. 1; CAA51229).
FT   CONFLICT    415    435       DADIVVTHASLEGRVKRVTDK -> GCRISGRLHPWPRSWK
FT                                GAVETGVRN (in Ref. 1; CAA51229).
SQ   SEQUENCE   462 AA;  48971 MW;  83F2D203D9E5A4C4 CRC64;
     MENKSARAKV QAFGGFLTAM VIPNIGAFIA WGFITALFIP TGWLPNEHFA KIVGPMITYL
     LPVMIGSTGG HLVGGKRGAV MGGIGTIGVI VGAEIPMFLG SMIMGPLGGL VIKYVDKALE
     KRIPAGFEMV INNFSLGIAG MLLCLLGFEV IGPAVLIANT FVKECIEALV HAGYLPLLSV
     INEPAKVLFL NNAIDQGVYY PLGMQQASVN GKSIFFMVAS NPGPGLGLLL AFTLFGKGMS
     KRSAPGAMII HFLGGIHELY FPYVLMKPLT IIAMIAGGMS GTWMFNLLDG GLVAGPSPGS
     IFAYLALTPK GSFLATIAGV TVGTLVSFAI TSLILKMEKT VETESEDEFA QSANAVKAMK
     QEGAFSLSRV KRIAFVCDAG MGSSAMGATT FRKRLEKAGL AIEVKHYAIE NVPADADIVV
     THASLEGRVK RVTDKPLILI NNYIGDPKLD TLFNQLTAEH KH
//
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