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 01-MAY-2013, entry version 67.
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RL Unpublished observations (JUN-1993).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 277:1453-1474(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;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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_000913.2.
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; MIVAMIA; -.
DR ProtClustDB; CLSK2460192; -.
DR BioCyc; EcoCyc:CMTA-MONOMER; -.
DR BioCyc; ECOL316407:JW2900-MONOMER; -.
DR BioCyc; MetaCyc:CMTA-MONOMER; -.
DR Genevestigator; P69826; -.
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 InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
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 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
//
