Conserved Protein Domain Family
PTS_IIB

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cd00133: PTS_IIB 
Click on image for an interactive view with Cn3D
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In the multienzyme PTS complex, EII is a carbohydrate-specific permease consisting of two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system. The PTS is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, polyols, amino sugars, and other sugar derivatives. The four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB), can phosphorylate or interact with numerous non-PTS proteins thereby regulating their activity.
Statistics
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PSSM-Id: 99904
View PSSM: cd00133
Aligned: 454 rows
Threshold Bit Score: 27.9906
Threshold Setting Gi: 15829222
Created: 2-May-2007
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:most of the active site residues are contained within a P-loop which forms part of a binding pocket for the phosphoryl group
  • Comment:for the E coli chitobiose transporter IIB subunit, in addition to the P-loop residues, two conserved residues are likely to be important in catalysis: a tyrosine whose side-chain points towards the phosphorylation site and a Gln residue whose side-chain lies close to the sulfur atom of the catalytic cysteine.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1             # ##  ##                                                                   
1TVM_A        23 KIIVACGGAvATSTMAAEEIKELCQSHNIp-VELIQCRvneietymDGVHLICTTarvdrsfgDIPLVHGmpfvsgvgie 101
gi 20806823  412 NVLVVCSTGiGTAKLLSSRLQSVFDVHII--DTIAFHQikev-lkdKKIDLIVSTipl--kcdEVKVVEVnpll----td 482
gi 148380105 407 NVLIVCATGiGTSKFISNKLKSIFDINII--DTISSHTmekilkynKNIDLIVTTipl--kvkGIKCIEVntfl----te 478
gi 20807093  416 NILVVCASGiGTSRMLMSKLQMFPQLNVV--EVASSVKlkel-ekrKDIDLIVSTipl--kltSKKVVVVnpll----le 486
gi 157691011 405 KAIIVCGSGlGTARLLEIKLKTAFQHELDivELYSYQDylm--sttLPCDVIITTvpl--askGKPVIQVsaff----eq 476
gi 133731169 409 SALIVCGSGfGTARIVEAKVKSAVSNLDIt-KVVSIQEynr--fihIEEDIILSTvri--pekNKPVIKIsnip----tn 479
gi 159874689 411 RAVVVCTTGlGTSVLLKAKLQSKTNLNIKvvGVYALYQldd--iefTDIDIIISTvpls-kkySIPDVVItpiv----sn 483
gi 145952933 401 KICIVCHYGiGTGQLISEKLKQNISDLSVv-GVYPVRYldm--aisQDVDLIVSTvel--kgyEKPVLYIenif----dd 471
gi 122090919 407 QVMLVCDTGnSTTRMIQAQISRKYPQIVMt-QTISLRDyen--ldhIDEDFIISNsrl--tekNKPVVVMspfp----te 477
gi 117617917 402 QALLLCDAGnATFRVLEARIKREYPQLQLt-MLESVRDyeg--larIEQDFVISTvka--gekNVPVVQVapfp----tq 472
                         90
                 ....*....|
Feature 1                  
1TVM_A       102 alQNKILTIL 111
gi 20806823  483 rdIEKLSKFL 492
gi 148380105 479 knISELGLYF 488
gi 20807093  487 edVEKLKKAL 496
gi 157691011 477 hdVQQVNEVI 486
gi 133731169 480 eeLKMLGAII 489
gi 159874689 484 ndIEKIHEFI 493
gi 145952933 472 slIENVNKAF 481
gi 122090919 478 yqLEQLGKLV 487
gi 117617917 473 yqLEQLGKLV 482

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