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 02-NOV-2016, entry version 157.
DE RecName: Full=PTS system maltose-specific EIICB component {ECO:0000303|PubMed:1856179};
DE Includes:
DE RecName: Full=Maltose permease IIC component {ECO:0000303|PubMed:1856179};
DE AltName: Full=PTS system maltose-specific EIIC component {ECO:0000303|PubMed:1856179};
DE Includes:
DE RecName: Full=Maltose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:1856179};
DE EC=2.7.1.208 {ECO:0000250|UniProtKB:P54715};
DE AltName: Full=PTS system maltose-specific EIIB component {ECO:0000303|PubMed:1856179};
GN Name=malX {ECO:0000303|PubMed:1856179};
GN OrderedLocusNames=b1621, JW1613;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY,
RP AND INDUCTION.
RC STRAIN=K12;
RX 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 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 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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX 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 transport. MalX can
CC also recognize and transport glucose even though this sugar may
CC not represent the natural substrate of the system.
CC {ECO:0000269|PubMed:1856179}.
CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine +
CC maltose(Side 1) = [protein]-L-histidine + maltose 6'-
CC phosphate(Side 2). {ECO:0000250|UniProtKB:P54715}.
CC -!- INTERACTION:
CC P21599:pykA; NbExp=3; IntAct=EBI-556578, EBI-368956;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: By maltose. Repressed by MalI.
CC {ECO:0000269|PubMed:1856179}.
CC -!- DOMAIN: The EIIC domain type-1 forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- DOMAIN: The PTS EIIB type-1 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-1 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00421}.
CC -!- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- SIMILARITY: Contains 1 PTS EIIC type-1 domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
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; NP_416138.1; NC_000913.3.
DR RefSeq; WP_000125583.1; NZ_LN832404.1.
DR ProteinModelPortal; P19642; -.
DR SMR; P19642; -.
DR BioGrid; 4261128; 20.
DR DIP; DIP-10150N; -.
DR IntAct; P19642; 1.
DR MINT; MINT-1239961; -.
DR STRING; 511145.b1621; -.
DR TCDB; 4.A.1.1.3; the pts glucose-glucoside (glc) family.
DR PaxDb; P19642; -.
DR PRIDE; P19642; -.
DR EnsemblBacteria; AAC74693; AAC74693; b1621.
DR EnsemblBacteria; BAA15372; BAA15372; BAA15372.
DR GeneID; 946009; -.
DR KEGG; ecj:JW1613; -.
DR KEGG; eco:b1621; -.
DR PATRIC; 32118544; VBIEscCol129921_1692.
DR EchoBASE; EB0558; -.
DR EcoGene; EG10563; malX.
DR eggNOG; ENOG4105CI1; Bacteria.
DR eggNOG; COG1263; LUCA.
DR eggNOG; COG1264; LUCA.
DR HOGENOM; HOG000250995; -.
DR InParanoid; P19642; -.
DR KO; K02790; -.
DR KO; K02791; -.
DR OMA; GTMDVCG; -.
DR PhylomeDB; P19642; -.
DR BioCyc; EcoCyc:MALX-MONOMER; -.
DR BioCyc; ECOL316407:JW1613-MONOMER; -.
DR BioCyc; MetaCyc:MALX-MONOMER; -.
DR PRO; PR:P19642; -.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009758; P:carbohydrate utilization; IGI:CACAO.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR011301; PTS_Mal/Glc-sp_IIBC_component.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 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 1: Evidence at protein level;
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 1 530 PTS system maltose-specific EIICB
FT component.
FT /FTId=PRO_0000186657.
FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 69 89 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 96 116 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 138 158 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 189 209 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 289 309 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 321 341 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 343 363 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 369 389 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT TRANSMEM 399 419 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT DOMAIN 1 431 PTS EIIC type-1. {ECO:0000255|PROSITE-
FT ProRule:PRU00426}.
FT DOMAIN 449 530 PTS EIIB type-1. {ECO:0000255|PROSITE-
FT ProRule:PRU00421}.
FT ACT_SITE 471 471 Phosphocysteine intermediate; for EIIB
FT activity. {ECO:0000255|PROSITE-
FT ProRule:PRU00421}.
FT CONFLICT 144 144 I -> Y (in Ref. 1; AAA24098).
FT {ECO:0000305}.
FT CONFLICT 296 296 P -> N (in Ref. 1; AAA24098).
FT {ECO:0000305}.
FT CONFLICT 432 432 E -> R (in Ref. 1; AAA24098).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 19 361 ipfam:PTS_EIIC [T]
FT MYHIT 9 431 iprf:PTS_EIIC_TYPE_1 [T]
FT MYHIT 464 481 ipat:PTS_EIIB_TYPE_1_CYS [T]
FT MYHIT 449 530 iprf:PTS_EIIB_TYPE_1 [T]
FT MYHIT 455 486 ipfam:PTS_EIIB [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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