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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   02-NOV-2016, entry version 97.
DE   RecName: Full=PTS system mannitol-specific cryptic EIICB component {ECO:0000303|PubMed:8353127};
DE   AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN   Name=cmtA {ECO:0000303|PubMed:8353127};
GN   OrderedLocusNames=b2933, JW2900;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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RL   Unpublished observations (JUN-1993).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. The enzyme II CmtAB PTS system is involved in D-mannitol
CC       transport. {ECO:0000250|UniProtKB:P28008}.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427, ECO:0000269|PubMed:15919996}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427,
CC       ECO:0000269|PubMed:15919996}.
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA51229.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the C-terminus.; Evidence={ECO:0000305};
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; WP_000428805.1; NZ_LN832404.1.
DR   ProteinModelPortal; P69826; -.
DR   SMR; P69826; -.
DR   BioGrid; 4262068; 76.
DR   IntAct; P69826; 3.
DR   STRING; 511145.b2933; -.
DR   TCDB; 4.A.2.1.24; the pts fructose-mannitol (fru) family.
DR   PaxDb; P69826; -.
DR   PRIDE; P69826; -.
DR   EnsemblBacteria; AAC75970; AAC75970; b2933.
DR   EnsemblBacteria; BAE76996; BAE76996; BAE76996.
DR   GeneID; 945256; -.
DR   KEGG; ecj:JW2900; -.
DR   KEGG; eco:b2933; -.
DR   PATRIC; 32121278; VBIEscCol129921_3027.
DR   EchoBASE; EB1740; -.
DR   EcoGene; EG11792; cmtA.
DR   eggNOG; ENOG4105CTS; Bacteria.
DR   eggNOG; COG2213; LUCA.
DR   HOGENOM; HOG000252814; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; DIVVTHE; -.
DR   PhylomeDB; P69826; -.
DR   BioCyc; EcoCyc:CMTA-MONOMER; -.
DR   BioCyc; ECOL316407:JW2900-MONOMER; -.
DR   BioCyc; MetaCyc:CMTA-MONOMER; -.
DR   PRO; PR:P69826; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISA:EcoCyc.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
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; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    462       PTS system mannitol-specific cryptic
FT                                EIICB component.
FT                                /FTId=PRO_0000186679.
FT   TOPO_DOM      1     24       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     25     46       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     47     50       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     51     71       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     72    134       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    135    156       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    157    165       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    166    186       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    187    273       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    274    293       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    294    313       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    314    335       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    336    462       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   DOMAIN       13    344       PTS EIIC type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN      371    461       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   ACT_SITE    377    377       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008}.
FT   MOD_RES     377    377       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008,
FT                                ECO:0000255|PROSITE-ProRule:PRU00422}.
FT   CONFLICT    274    275       MI -> IEF (in Ref. 1; CAA51229).
FT                                {ECO:0000305}.
FT   CONFLICT    415    435       DADIVVTHASLEGRVKRVTDK -> GCRISGRLHPWPRSWK
FT                                GAVETGVRN (in Ref. 1; CAA51229).
FT                                {ECO:0000305}.
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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