PTMCB_ECOLI
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 03-AUG-2022, entry version 121.
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}; 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 Gram-
RT 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RL Unpublished observations (JUN-1993).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., 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 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. The
CC enzyme II CmtAB PTS system is involved in D-mannitol transport.
CC {ECO:0000250|UniProtKB:P28008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannitol 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC ChEBI:CHEBI:64837; EC=2.7.1.197;
CC Evidence={ECO:0000250|UniProtKB:P00550};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC 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-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-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51229.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the C-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; 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; 66673186; -.
DR GeneID; 945256; -.
DR KEGG; ecj:JW2900; -.
DR KEGG; eco:b2933; -.
DR PATRIC; fig|1411691.4.peg.3800; -.
DR EchoBASE; EB1740; -.
DR eggNOG; COG2213; Bacteria.
DR HOGENOM; CLU_028721_2_0_6; -.
DR OMA; FVAFACD; -.
DR PhylomeDB; P69826; -.
DR BioCyc; EcoCyc:CMTA-MON; -.
DR BioCyc; MetaCyc:CMTA-MON; -.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
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; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..462
FT /note="PTS system mannitol-specific cryptic EIICB
FT component"
FT /id="PRO_0000186679"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 47..50
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 72..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 157..165
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 187..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 294..313
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 336..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 13..344
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 371..461
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 377
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008"
FT MOD_RES 377
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT ProRule:PRU00422"
FT CONFLICT 274..275
FT /note="MI -> IEF (in Ref. 1; CAA51229)"
FT /evidence="ECO:0000305"
FT CONFLICT 415..435
FT /note="DADIVVTHASLEGRVKRVTDK -> GCRISGRLHPWPRSWKGAVETGVRN
FT (in Ref. 1; CAA51229)"
FT /evidence="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
