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Conserved domains on  [gi|730234113|ref|WP_033939433|]
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MULTISPECIES: energy transducer TonB [Pseudomonas]

Protein Classification

energy transducer TonB( domain architecture ID 10507740)

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.)

CATH:  3.30.1150.10
Gene Ontology:  GO:0015031|GO:0031992|GO:0055085|GO:0015891|GO:0030288

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TonB_C pfam03544
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ...
 193-271 5.41e-27

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: 100.05  E-value: 5.41e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730234113  193 PAPEYPALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKL 271
Cdd:pfam03544   1 PEPVYPEEARRRGIEGTVVVEFLIDPDGNVTNVRVVKSSGYSILDEAALEAVKKWRFKPAPKNGQPVTVEITVPIRFKL 79
 
Name Accession Description Interval E-value
TonB_C pfam03544
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ...
 193-271 5.41e-27

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: 100.05  E-value: 5.41e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730234113  193 PAPEYPALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKL 271
Cdd:pfam03544   1 PEPVYPEEARRRGIEGTVVVEFLIDPDGNVTNVRVVKSSGYSILDEAALEAVKKWRFKPAPKNGQPVTVEITVPIRFKL 79
tonB_Cterm TIGR01352
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ...
 199-272 5.91e-24

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: 91.98  E-value: 5.91e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730234113  199 ALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKLN 272
Cdd:TIGR01352   1 ARARRRGIEGTVVVRFTVDPSGRVTSVSVLKSSGDRALDRAALEAVRKARFEPPPPPGGVVAASVTIPVRFKLP 74
TonB COG0810
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ...
 198-268 6.31e-19

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


Pssm-ID: 440572 [Multi-domain]  Cd Length: 70  Bit Score: 78.40  E-value: 6.31e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730234113 198 PALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVsVPID 268
Cdd:COG0810    1 PEEARRRGIEGTVTVRFTIDADGRVTDVEVVKSSGHPLLDEAALRAVRRWRFKPAKQNGKPVRVKT-VPIR 70
myxo_SS_tail NF033768
AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM ...
 207-270 5.02e-03

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: 35.62  E-value: 5.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730234113 207 EGTVLLRVHVLASGSPSEIQVQKSS-GREALDQAAVKAVKRWSFvPAKRGDKAEdgwVSVPIDFK 270
Cdd:NF033768  32 AGKVVVEFTIGPSGRVSSVKVVSSTlKDPKVESCILRRIKRWRF-PKPKGGEVT---VTYPFIFS 92
 
Name Accession Description Interval E-value
TonB_C pfam03544
Gram-negative bacterial TonB protein C-terminal; The TonB_C domain is the well-characterized ...
 193-271 5.41e-27

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: 100.05  E-value: 5.41e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730234113  193 PAPEYPALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKL 271
Cdd:pfam03544   1 PEPVYPEEARRRGIEGTVVVEFLIDPDGNVTNVRVVKSSGYSILDEAALEAVKKWRFKPAPKNGQPVTVEITVPIRFKL 79
tonB_Cterm TIGR01352
TonB family C-terminal domain; This model represents the C-terminal of TonB and is homologs. ...
 199-272 5.91e-24

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: 91.98  E-value: 5.91e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730234113  199 ALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKLN 272
Cdd:TIGR01352   1 ARARRRGIEGTVVVRFTVDPSGRVTSVSVLKSSGDRALDRAALEAVRKARFEPPPPPGGVVAASVTIPVRFKLP 74
TonB COG0810
Periplasmic protein TonB, links inner and outer membranes [Cell wall/membrane/envelope ...
 198-268 6.31e-19

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


Pssm-ID: 440572 [Multi-domain]  Cd Length: 70  Bit Score: 78.40  E-value: 6.31e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730234113 198 PALAMRRGWEGTVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVsVPID 268
Cdd:COG0810    1 PEEARRRGIEGTVTVRFTIDADGRVTDVEVVKSSGHPLLDEAALRAVRRWRFKPAKQNGKPVRVKT-VPIR 70
TonB_2 pfam13103
TonB C terminal; This family contains TonB members that are not captured by pfam03544.
 209-267 8.18e-05

TonB C terminal; This family contains TonB members that are not captured by pfam03544.


Pssm-ID: 463788 [Multi-domain]  Cd Length: 85  Bit Score: 40.39  E-value: 8.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 730234113  209 TVLLRVHVLASGSPSEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPI 267
Cdd:pfam13103  27 EAVVEITIDPDGTIVSVRLVKSSGNEAFDKAVLRALEKSSPLPPPPEYGGVPREIGFTF 85
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 209-271 8.64e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730234113  209 TVLLRVHVLASGSpsEIQVQKSSGREALDQAAVKAVKRWSFVPAKRGDKAEDGWVSVPIDFKL 271
Cdd:TIGR02794 286 TCRLRIRLAPDGT--LLSVTKSSGDPALCQAALAAVAKAAKLPMPPSDPVYEEFKNINLTFKP 346
myxo_SS_tail NF033768
AgmX/PglI C-terminal domain; The AgmX/PglI C-terminal domain described by this HMM ...
 207-270 5.02e-03

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: 35.62  E-value: 5.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730234113 207 EGTVLLRVHVLASGSPSEIQVQKSS-GREALDQAAVKAVKRWSFvPAKRGDKAEdgwVSVPIDFK 270
Cdd:NF033768  32 AGKVVVEFTIGPSGRVSSVKVVSSTlKDPKVESCILRRIKRWRF-PKPKGGEVT---VTYPFIFS 92
 
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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