ID PTOCB_ECOLI Reviewed; 530 AA.
AC P19642; P77621;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-NOV-2009, entry version 101.
DE RecName: Full=PTS system maltose- and glucose-specific EIICB component;
DE Includes:
DE RecName: Full=Maltose and glucose permease IIC component;
DE AltName: Full=PTS system maltose- and glucose-specific EIIC component;
DE Includes:
DE RecName: Full=Maltose- and glucose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.69;
DE AltName: Full=PTS system maltose- and glucose-specific EIIB component;
GN Name=malX; OrderedLocusNames=b1621, JW1613;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=91310596; PubMed=1856179;
RA Reidl J., Boos W.;
RT "The malX malY operon of Escherichia coli encodes a novel enzyme II of
RT the phosphotransferase system recognizing glucose and maltose and an
RT enzyme abolishing the endogenous induction of the maltose system.";
RL J. Bacteriol. 173:4862-4876(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX MEDLINE=97426617; 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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX MEDLINE=89359124; PubMed=2670898;
RA Reidl J., Roemisch K., Ehrmann M., Boos W.;
RT "MalI, a novel protein involved in regulation of the maltose system of
RT Escherichia coli, is highly homologous to the repressor proteins GalR,
RT CytR, and LacI.";
RL J. Bacteriol. 171:4888-4899(1989).
RN [6]
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 maltose and glucose
CC transport.
CC -!- FUNCTION: MalX encodes a phosphotransferase system enzyme II that
CC can recognize glucose and maltose as substrates even though these
CC sugars may not represent the natural substrates of the system.
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-1 domain.
CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
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DR EMBL; M60722; AAA24098.1; -; mRNA.
DR EMBL; U00096; AAC74693.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15372.1; -; Genomic_DNA.
DR EMBL; M28539; AAA24103.2; ALT_SEQ; Genomic_DNA.
DR PIR; G64918; G64918.
DR RefSeq; AP_002242.1; -.
DR RefSeq; NP_416138.1; -.
DR HSSP; P05053; 1IBA.
DR DIP; DIP:10150N; -.
DR STRING; P19642; -.
DR TCDB; 4.A.1.1.3; PTS glucose-glucoside (Glc) family.
DR GeneID; 946009; -.
DR GenomeReviews; AP009048_GR; JW1613.
DR GenomeReviews; U00096_GR; b1621.
DR KEGG; ecj:JW1613; -.
DR KEGG; eco:b1621; -.
DR EchoBASE; EB0558; -.
DR EcoGene; EG10563; malX.
DR HOGENOM; P19642; -.
DR OMA; IFGTGER; -.
DR BioCyc; EcoCyc:MALX-MON; -.
DR Genevestigator; P19642; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosph...; IEA:EC.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phospho...; IEA:UniProtKB-KW.
DR InterPro; IPR018113; PTrfase_EIIB/Cys_phosph_CS.
DR InterPro; IPR004719; PTrfase_sys_maltose/Glc-sp_IIC.
DR InterPro; IPR001996; PTS_EIIB.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR011535; PTS_Glc-like_IIB_component.
DR InterPro; IPR011301; PTS_Mal/Glc-sp_IIBC_component.
DR Gene3D; G3DSA:3.30.1360.60; PTS_EIIB; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02004; PTS-IIBC-malX; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Complete proteome; Kinase;
KW Membrane; Phosphotransferase system; Sugar transport; Transferase;
KW Transmembrane; Transport.
FT CHAIN 1 530 PTS system maltose- and glucose-specific
FT EIICB component.
FT /FTId=PRO_0000186657.
FT TRANSMEM 22 42 Potential.
FT TRANSMEM 69 89 Potential.
FT TRANSMEM 96 116 Potential.
FT TRANSMEM 138 158 Potential.
FT TRANSMEM 189 209 Potential.
FT TRANSMEM 289 309 Potential.
FT TRANSMEM 321 341 Potential.
FT TRANSMEM 343 363 Potential.
FT TRANSMEM 369 389 Potential.
FT TRANSMEM 399 419 Potential.
FT DOMAIN 1 431 PTS EIIC type-1.
FT DOMAIN 449 530 PTS EIIB type-1.
FT ACT_SITE 471 471 Phosphocysteine intermediate; for EIIB
FT activity (By similarity).
FT CONFLICT 144 144 I -> Y (in Ref. 1; AAA24098).
FT CONFLICT 296 296 P -> N (in Ref. 1; AAA24098).
FT CONFLICT 432 432 E -> R (in Ref. 1; AAA24098).
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 19 361 ipfam:PTS_EIIC [T]
FT MYHIT 464 481 ipat:PTS_EIIB_TYPE_1_CYS [T]
FT MYHIT 455 486 ipfam:PTS_EIIB [T]
FT MYHIT 9 431 iprf:PTS_EIIC_TYPE_1 [T]
FT MYHIT 449 530 iprf:PTS_EIIB_TYPE_1 [T]
SQ SEQUENCE 530 AA; 56627 MW; 042E9817955975BF CRC64;
MTAKTAPKVT LWEFFQQLGK TFMLPVALLS FCGIMLGIGS SLSSHDVITL IPVLGNPVLQ
AIFTWMSKIG SFAFSFLPVM FCIAIPLGLA RENKGVAAFA GFIGYAVMNL AVNFWLTNKG
ILPTTDAAVL KANNIQSILG IQSIDTGILG AVIAGIIVWM LHERFHNIRL PDALAFFGGT
RFVPIISSLV MGLVGLVIPL VWPIFAMGIS GLGHMINSAG DFGPMLFGTG ERLLLPFGLH
HILVALIRFT DAGGTQEVCG QTVSGALTIF QAQLSCPTTH GFSESATRFL SQGKMPAFLG
GLPGAALAMY HCARPENRHK IKGLLISGLI ACVVGGTTEP LEFLFLFVAP VLYVIHALLT
GLGFTVMSVL GVTIGNTDGN IIDFVVFGIL HGLSTKWYMV PVVAAIWFVV YYVIFRFAIT
RFNLKTPGRD SEVASSIEKA VAGAPGKSGY NVPAILEALG GADNIVSLDN CITRLRLSVK
DMSLVNVQAL KDNRAIGVVQ LNQHNLQVVI GPQVQSVKDE MAGLMHTVQA
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