NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|581494081|gb|EVP02942|]
View 

hypothetical protein P140_02619 [Staphylococcus aureus M1094]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 1-140 7.11e-40

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


The actual alignment was detected with superfamily member cd01138:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 248  Bit Score: 134.77  E-value: 7.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIGqATASVFEPDE-KQIYIYNStWGRGLDIVHDAF-GMPMTKQYKDklQED 78
Cdd:cd01138  109 LLNKEDEAEKWLADYKQKAKEAKEKIKKKLG-NDKSVAVLRGrKQIYVFGE-DGRGGGPILYADlGLKAPEKVKE--IED 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581494081  79 KKGYASISKENISKYAGDYIFLSKP--SYGKFDFEKTHTWQNIEAVKKGHVISYKAEDYWFTDP 140
Cdd:cd01138  185 KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG 248
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 1-140 7.11e-40

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 134.77  E-value: 7.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIGqATASVFEPDE-KQIYIYNStWGRGLDIVHDAF-GMPMTKQYKDklQED 78
Cdd:cd01138  109 LLNKEDEAEKWLADYKQKAKEAKEKIKKKLG-NDKSVAVLRGrKQIYVFGE-DGRGGGPILYADlGLKAPEKVKE--IED 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581494081  79 KKGYASISKENISKYAGDYIFLSKP--SYGKFDFEKTHTWQNIEAVKKGHVISYKAEDYWFTDP 140
Cdd:cd01138  185 KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG 248
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 1-133 1.82e-29

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 107.45  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081    1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIgQATASVFEPDEKQIYIYNSTWGRGLDIVHDAFGMPMTKQYkdklqeDKK 80
Cdd:pfam01497 104 LLGLEDEAEELVAEIDSALAAAKKAVPSLT-RKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIENIAAEL------SGS 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581494081   81 GYASISKENISKYAGDYIFLSKP----SYGKFDFEKTHTWQNIEAVKKGHVISYKAE 133
Cdd:pfam01497 177 EYAPISFEAILSSNPDVIIVSGRdsftKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 1-155 8.90e-13

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 63.86  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIGQATASVFEPDEKQIYIYNSTWGRGlDIVHDAfGMpmtkqyKDKLQEDKK 80
Cdd:COG0614  107 LLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG-ELLELA-GG------RNVAADLGG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081  81 GYASISKENISKYAGDYIFLSKPSYGKFDFEKTHT-------WQNIEAVKKGHVISYKAEDYWFTDPIT---LEHLRSKL 150
Cdd:COG0614  179 GYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEalladpgWQSLPAVKNGRVYVVPGDLLSRPGPRLllaLEDLAKAL 258


                 ....*
gi 581494081 151 KKEIL 155
Cdd:COG0614  259 HPELF 263
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 1-140 7.11e-40

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 134.77  E-value: 7.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIGqATASVFEPDE-KQIYIYNStWGRGLDIVHDAF-GMPMTKQYKDklQED 78
Cdd:cd01138  109 LLNKEDEAEKWLADYKQKAKEAKEKIKKKLG-NDKSVAVLRGrKQIYVFGE-DGRGGGPILYADlGLKAPEKVKE--IED 184

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581494081  79 KKGYASISKENISKYAGDYIFLSKP--SYGKFDFEKTHTWQNIEAVKKGHVISYKAEDYWFTDP 140
Cdd:cd01138  185 KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG 248
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 1-133 1.82e-29

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 107.45  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081    1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIgQATASVFEPDEKQIYIYNSTWGRGLDIVHDAFGMPMTKQYkdklqeDKK 80
Cdd:pfam01497 104 LLGLEDEAEELVAEIDSALAAAKKAVPSLT-RKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIENIAAEL------SGS 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581494081   81 GYASISKENISKYAGDYIFLSKP----SYGKFDFEKTHTWQNIEAVKKGHVISYKAE 133
Cdd:pfam01497 177 EYAPISFEAILSSNPDVIIVSGRdsftKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 1-155 8.90e-13

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 63.86  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   1 MTNNEDKAKKWIEEWDDKTRKDKKEIQSKIGQATASVFEPDEKQIYIYNSTWGRGlDIVHDAfGMpmtkqyKDKLQEDKK 80
Cdd:COG0614  107 LLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG-ELLELA-GG------RNVAADLGG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081  81 GYASISKENISKYAGDYIFLSKPSYGKFDFEKTHT-------WQNIEAVKKGHVISYKAEDYWFTDPIT---LEHLRSKL 150
Cdd:COG0614  179 GYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEalladpgWQSLPAVKNGRVYVVPGDLLSRPGPRLllaLEDLAKAL 258


                 ....*
gi 581494081 151 KKEIL 155
Cdd:COG0614  259 HPELF 263
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 2-129 4.66e-11

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 59.16  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   2 TNNEDKAKKWIEEWDDKTRKDKKEIQSKIGQATASV--FEPDEKQIYIYNSTWGrgldIVHDAFGMPMTKQYKDKlqeDK 79
Cdd:COG4594  162 LGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVgqFRADGLRLYTPNSFAG----SVLAALGFENPPKQSKD---NG 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 581494081  80 KGYASISKENISKYAGDYIFLSKPSYGKF--DFEKTHTWQNIEAVKKGHVIS 129
Cdd:COG4594  235 YGYSEVSLEQLPALDPDVLFIATYDDPSIlkEWKNNPLWKNLKAVKNGRVYE 286
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 2-136 5.61e-11

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 58.84  E-value: 5.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   2 TNNEDKAKKWIEEWDDKTRKDKKEIQSKIGQATASVFEPDEKQIYIYNSTWGRGlDIVHDA-FGMPMTKQykdklQEDKK 80
Cdd:cd01146  112 LGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLYGPNSFAG-SVLEDLgLQNPWAQE-----TTNDS 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 581494081  81 GYASISKENISKYAGDYIFLS--KPSYGKFDFEKTHTWQNIEAVKKGHVisYKAEDYW 136
Cdd:cd01146  186 GFATISLERLAKADADVLFVFtyEDEELAQALQANPLWQNLPAVKNGRV--YVVDDVW 241
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 3-127 2.82e-03

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 36.93  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   3 NNEDKAKK---WIEE-WDDKTRKDKKEIQSK--------IGQATASVFEPDEKqIYIYNSTWGRGLDIVHDAfgmpmtkq 70
Cdd:cd01147  125 GKEERAEElisFIESiLADVEERTKDIPDEEkptvyfgrIGTKGAAGLESGLA-GSIEVFELAGGINVADGL-------- 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081  71 ykdklqeDKKGYASISKENISKYAGDYIFLSKPSYGKFDFEKTHT---WQNIEAVKKGHV 127
Cdd:cd01147  196 -------GGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKNrpfWQSLKAVKNGRV 248
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 2-137 2.90e-03

Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 36.95  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   2 TNNEDKAKKWIEEWDDKtrkdkkeiQSKIGQATASVFEPDEKQIYIYN----STWGRGL---DIVHDAFGMPMTKQYKDk 74
Cdd:cd01142  134 LGRQEKAEALVAYFDDN--------LAYVAARTKKLPDSERPRVYYAGpdplTTDGTGSitnSWIDLAGGINVASEATK- 204

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581494081  75 lqedkKGYASISKENISKYAGDYIFLSKPsYGKFDFEKTHTWQNIEAVKKGHVisYKAEDYWF 137
Cdd:cd01142  205 -----KGSGEVSLEQLLKWNPDVIIVGNA-DTKAAILADPRWQNLRAVKNGRV--YVNPEGAF 259
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 3-136 3.10e-03

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 36.47  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581494081   3 NNEDKAKKWIEEWDDKTRKDKKEIQSKiGQATASVFEPDEKQIYIYNSTWGrgldIVHDAFGMPMTkqykDKLQEDKKGY 82
Cdd:cd01140  121 GKEEEAKELVAEIDASIAEAKSAAKGK-KKALVVLVNGGKLSAFGPGSRFG----WLHDLLGFEPA----DENIKASSHG 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581494081  83 ASISKENISKYAGDYIFL---SKPSYGKFDFEKTH----TWQNIEAVKKGHVIsYKAEDYW 136
Cdd:cd01140  192 QPVSFEYILEANPDWLFVidrGAAIGAEGSSAKEVldndLVKNTTAWKNGKVI-YLDPDLW 251
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH