PTOCB_ECOLI
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-AUG-2022, entry version 186.
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}; 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, AND
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=1856179; DOI=10.1128/jb.173.15.4862-4876.1991;
RA Reidl J., Boos W.;
RT "The malX malY operon of Escherichia coli encodes a novel enzyme II of the
RT phosphotransferase system recognizing glucose and maltose and an enzyme
RT 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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
RX PubMed=2670898; DOI=10.1128/jb.171.9.4888-4899.1989;
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 phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in maltose transport. MalX can also recognize and
CC transport glucose even though this sugar may not represent the natural
CC substrate of the system. {ECO:0000269|PubMed:1856179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha-
CC maltose 6'-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49300, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:17306, ChEBI:CHEBI:29979, ChEBI:CHEBI:57478,
CC ChEBI:CHEBI:64837; EC=2.7.1.208;
CC Evidence={ECO:0000250|UniProtKB:P54715};
CC -!- INTERACTION:
CC P19642; P21599: pykA; NbExp=4; IntAct=EBI-556578, EBI-368956;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: By maltose. Repressed by MalI. {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-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00421}.
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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; NP_416138.1; NC_000913.3.
DR RefSeq; WP_000125583.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P19642; -.
DR SMR; P19642; -.
DR BioGRID; 4261128; 34.
DR BioGRID; 850370; 1.
DR DIP; DIP-10150N; -.
DR IntAct; P19642; 1.
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; fig|1411691.4.peg.640; -.
DR EchoBASE; EB0558; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR InParanoid; P19642; -.
DR OMA; TATKWYL; -.
DR PhylomeDB; P19642; -.
DR BioCyc; EcoCyc:MALX-MON; -.
DR BioCyc; MetaCyc:MALX-MON; -.
DR PHI-base; PHI:4631; -.
DR PRO; PR:P19642; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0090564; F:protein-phosphocysteine-glucose phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009758; P:carbohydrate utilization; IGI:CACAO.
DR GO; GO:1904659; P:glucose transmembrane transport; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
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; Kinase; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="PTS system maltose-specific EIICB component"
FT /id="PRO_0000186657"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..431
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 449..530
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 471
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT CONFLICT 144
FT /note="I -> Y (in Ref. 1; AAA24098)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="P -> N (in Ref. 1; AAA24098)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> R (in Ref. 1; AAA24098)"
FT /evidence="ECO:0000305"
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
