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Conserved domains on  [gi|110590399]
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Chain C, Protein tonB

Protein Classification

energy transducer TonB( domain architecture ID 11484971)

energy transducer TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10819 PRK10819
transport protein TonB; Provisional
 21-229 7.46e-82

transport protein TonB; Provisional


:

Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 244.59  E-value: 7.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  21 SVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPK----PVKKV 96
Cdd:PRK10819  34 SVHQVIELPAPAQPISVTMVAPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKpkpkPVKKV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  97 QEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDG 176
Cdd:PRK10819 114 EEQPKREVKPVEPRPASPFENTAPARPTSSTATAAASKPVTSVSSGPRALSRNQPQYPARAQALRIEGQVKVKFDVDEDG 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110590399 177 RVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ 229
Cdd:PRK10819 194 RVDNVRILSAEPRNMFEREVKQAMRKWRYEAGKPGKGLVVNIVFKINGTTEIE 246
 
Name Accession Description Interval E-value
PRK10819 PRK10819
transport protein TonB; Provisional
 21-229 7.46e-82

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 244.59  E-value: 7.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  21 SVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPK----PVKKV 96
Cdd:PRK10819  34 SVHQVIELPAPAQPISVTMVAPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKpkpkPVKKV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  97 QEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDG 176
Cdd:PRK10819 114 EEQPKREVKPVEPRPASPFENTAPARPTSSTATAAASKPVTSVSSGPRALSRNQPQYPARAQALRIEGQVKVKFDVDEDG 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110590399 177 RVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ 229
Cdd:PRK10819 194 RVDNVRILSAEPRNMFEREVKQAMRKWRYEAGKPGKGLVVNIVFKINGTTEIE 246
TonB_C pfam03544
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ...
 150-222 7.64e-20

Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.


Pssm-ID: 427361 [Multi-domain]  Cd Length: 79  Bit Score: 80.41  E-value: 7.64e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110590399  150 QPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPG-----SGIVVNILFKI 222
Cdd:pfam03544   2 EPVYPEEARRRGIEGTVVVEFLIDPDGNVTNVRVVKSSGYSILDEAALEAVKKWRFKPAPKNgqpvtVEITVPIRFKL 79
tonB_Cterm TIGR01352
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ...
 155-223 1.11e-16

TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273570 [Multi-domain]  Cd Length: 74  Bit Score: 71.95  E-value: 1.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110590399  155 ARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSG-----IVVNILFKIN 223
Cdd:TIGR01352   1 ARARRRGIEGTVVVRFTVDPSGRVTSVSVLKSSGDRALDRAALEAVRKARFEPPPPPGGvvaasVTIPVRFKLP 74
TonB COG0810
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ...
 154-209 8.37e-15

Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440572 [Multi-domain]  Cd Length: 70  Bit Score: 66.84  E-value: 8.37e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 110590399 154 PARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGK 209
Cdd:COG0810    1 PEEARRRGIEGTVTVRFTIDADGRVTDVEVVKSSGHPLLDEAALRAVRRWRFKPAK 56
myxo_SS_tail NF033768
AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM ...
 144-216 1.26e-05

AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM (myxo_SS_tail) occurs as the C-terminal domain in multiple proteins per genome for a number of species capable of surface gliding motility, e.g. 12 in Myxococcus xanthus. Member proteins include the adventurous gliding motility proteins AgmX (GltJ) and PglI in M. xanthus. The domain is about 92 amino acids long, and features a pair of Cys residues about 45 amino acids apart in almost all cases.


Pssm-ID: 468180  Cd Length: 92  Bit Score: 42.56  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110590399 144 RALSRNQP--QYPARAQALR---IEGQVKVKFDVTPDGRVDNVQIL-SAKPANMFEREVKNAMRRWRYEPGKPGSGIVV 216
Cdd:NF033768   8 RVVRAHLGeiRYCYERELKRnpsLAGKVVVEFTIGPSGRVSSVKVVsSTLKDPKVESCILRRIKRWRFPKPKGGEVTVT 86
 
Name Accession Description Interval E-value
PRK10819 PRK10819
transport protein TonB; Provisional
 21-229 7.46e-82

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 244.59  E-value: 7.46e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  21 SVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPK----PVKKV 96
Cdd:PRK10819  34 SVHQVIELPAPAQPISVTMVAPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIPKPEPKPKPKPKpkpkPVKKV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399  97 QEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDG 176
Cdd:PRK10819 114 EEQPKREVKPVEPRPASPFENTAPARPTSSTATAAASKPVTSVSSGPRALSRNQPQYPARAQALRIEGQVKVKFDVDEDG 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110590399 177 RVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ 229
Cdd:PRK10819 194 RVDNVRILSAEPRNMFEREVKQAMRKWRYEAGKPGKGLVVNIVFKINGTTEIE 246
TonB_C pfam03544
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ...
 150-222 7.64e-20

Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.


Pssm-ID: 427361 [Multi-domain]  Cd Length: 79  Bit Score: 80.41  E-value: 7.64e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110590399  150 QPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPG-----SGIVVNILFKI 222
Cdd:pfam03544   2 EPVYPEEARRRGIEGTVVVEFLIDPDGNVTNVRVVKSSGYSILDEAALEAVKKWRFKPAPKNgqpvtVEITVPIRFKL 79
tonB_Cterm TIGR01352
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ...
 155-223 1.11e-16

TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273570 [Multi-domain]  Cd Length: 74  Bit Score: 71.95  E-value: 1.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110590399  155 ARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSG-----IVVNILFKIN 223
Cdd:TIGR01352   1 ARARRRGIEGTVVVRFTVDPSGRVTSVSVLKSSGDRALDRAALEAVRKARFEPPPPPGGvvaasVTIPVRFKLP 74
TonB COG0810
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ...
 154-209 8.37e-15

Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440572 [Multi-domain]  Cd Length: 70  Bit Score: 66.84  E-value: 8.37e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 110590399 154 PARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGK 209
Cdd:COG0810    1 PEEARRRGIEGTVTVRFTIDADGRVTDVEVVKSSGHPLLDEAALRAVRRWRFKPAK 56
TonB_N pfam16031
TonB polyproline region; TonB from Escherichia coli and its homologs are critical for the ...
 23-147 9.26e-11

TonB polyproline region; TonB from Escherichia coli and its homologs are critical for the uptake of siderophores through the outer membrane of Gram-negative bacteria using chemiosmotic energy. The proline-rich segment of TonB exists in a PPII-like conformation. The result implies that the proline-rich segment of TonB possesses a length of more than 15 nm, sufficient to span the periplasm of Gram-negative bacteria.


Pssm-ID: 435086 [Multi-domain]  Cd Length: 136  Bit Score: 57.72  E-value: 9.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110590399   23 HQVIELPAPAQ-PISVTMVTPADLEPPQ----AVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKpkPKPKPV---K 94
Cdd:pfam16031   1 HQVIELPSPAQqPISVTMVNPADLEPPPpaapAPQPAPEPVVEPEPEPEPEPLPEPPAPVVIHKPKPK--PKPKPKpkpV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110590399   95 KVQEQPKRDVKPVESRPASPFEN-----TAPARLTSSTATAATSKPVTSVASGPRALS 147
Cdd:pfam16031  79 KKVEVPKREVKPVEPRPESPFENapsalVAPARPVSSTATAATASPSVSSASGPRALS 136
myxo_SS_tail NF033768
AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM ...
 144-216 1.26e-05

AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM (myxo_SS_tail) occurs as the C-terminal domain in multiple proteins per genome for a number of species capable of surface gliding motility, e.g. 12 in Myxococcus xanthus. Member proteins include the adventurous gliding motility proteins AgmX (GltJ) and PglI in M. xanthus. The domain is about 92 amino acids long, and features a pair of Cys residues about 45 amino acids apart in almost all cases.


Pssm-ID: 468180  Cd Length: 92  Bit Score: 42.56  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110590399 144 RALSRNQP--QYPARAQALR---IEGQVKVKFDVTPDGRVDNVQIL-SAKPANMFEREVKNAMRRWRYEPGKPGSGIVV 216
Cdd:NF033768   8 RVVRAHLGeiRYCYERELKRnpsLAGKVVVEFTIGPSGRVSSVKVVsSTLKDPKVESCILRRIKRWRFPKPKGGEVTVT 86
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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