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Conserved domains on  [gi|1028197998|ref|WP_063942036|]
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MULTISPECIES: zinc resistance sensor/chaperone ZraP [Citrobacter]

Protein Classification

zinc resistance sensor/chaperone ZraP( domain architecture ID 10013828)

zinc resistance sensor/chaperone ZraP is a periplasmic protein that could be an important component of the zinc-balancing mechanism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zraP PRK11546
zinc resistance sensor/chaperone ZraP;
1-147 1.50e-65

zinc resistance sensor/chaperone ZraP;


:

Pssm-ID: 183189  Cd Length: 143  Bit Score: 195.84  E-value: 1.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   1 MKRNNK--LALIALSLIALGSTPVLAQNHWGYGDGMQQRGGTPMTAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNAL 78
Cdd:PRK11546    1 MKRNTKiaLVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028197998  79 LTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVPRgagmgyGGCGGGGNHRSGGHMGMGHW 147
Cdd:PRK11546   81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPR------GAGMGYGGCGGGGHMGMGHW 143
 
Name Accession Description Interval E-value
zraP PRK11546
zinc resistance sensor/chaperone ZraP;
1-147 1.50e-65

zinc resistance sensor/chaperone ZraP;


Pssm-ID: 183189  Cd Length: 143  Bit Score: 195.84  E-value: 1.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   1 MKRNNK--LALIALSLIALGSTPVLAQNHWGYGDGMQQRGGTPMTAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNAL 78
Cdd:PRK11546    1 MKRNTKiaLVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028197998  79 LTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVPRgagmgyGGCGGGGNHRSGGHMGMGHW 147
Cdd:PRK11546   81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPR------GAGMGYGGCGGGGHMGMGHW 143
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
 3-120 1.73e-17

Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 73.48  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   3 RNNKLALIALSLIALGSTPVLAQNHWGYGDGMqqRGGTPM------TAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYN 76
Cdd:COG3678     2 KLKLLALLLALALALGAASAFAAGPPGGPRGG--RGLRRMleglnlTEEQRQQIRAIRQQYRKQMRALRQQLREAREELR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1028197998  77 ALLTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVP 120
Cdd:COG3678    80 ALLAADKFDEAAVRALADKIAALRAQLAVERAEARNQMYKVLTP 123
Metal_resist pfam13801
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ...
 7-121 7.75e-16

Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.


Pssm-ID: 433488 [Multi-domain]  Cd Length: 119  Bit Score: 68.86  E-value: 7.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   7 LALIALSLIALGSTPVLAQNHWGYG--DGMQQRGGTPMTAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNALLTASSP 84
Cdd:pfam13801   2 LNLFLLGALVGAALRGPGGPPGGGPgrGGMLLRAALGLPAEQRERLRAALRDHARELRALRRELRAARRELAALLAAPPF 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1028197998  85 DTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVPR 121
Cdd:pfam13801  82 DPAAIEAALAEARQARAALQAQIEEALLEFAATLSPE 118
CpxP_like cd09916
CpxP component of the bacterial Cpx-two-component system and related proteins; This family ...
 43-116 3.48e-06

CpxP component of the bacterial Cpx-two-component system and related proteins; This family summarizes bacterial proteins related to CpxP, a periplasmic protein that forms part of a two-component system which acts as a global modulator of cell-envelope stress in gram-negative bacteria. CpxP aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to alkaline pH. Functioning as a dimer, it inhibits activation of the kinase CpxA, but also plays a vital role in the quality control system of P pili. It has been suggested that CpxP directly interacts with CpxA via its concave polar surface. Another member of this family, Spy, is also a periplasmic protein that may be involved in the response to stress. The homology between CpxP and Spy suggests similar functions. A characteristic 5-residue sequence motif LTXXQ is found repeated twice in many members of this family.


Pssm-ID: 197366 [Multi-domain]  Cd Length: 96  Bit Score: 42.97  E-value: 3.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028197998  43 TAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNALLTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQ 116
Cdd:cd09916     5 TDEQKAQIKAIRQAARAQMKALREQMRAAREELRALLTADTFDEAAVRALAAEMAELQQELAVERAKARNQIYQ 78
 
Name Accession Description Interval E-value
zraP PRK11546
zinc resistance sensor/chaperone ZraP;
1-147 1.50e-65

zinc resistance sensor/chaperone ZraP;


Pssm-ID: 183189  Cd Length: 143  Bit Score: 195.84  E-value: 1.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   1 MKRNNK--LALIALSLIALGSTPVLAQNHWGYGDGMQQRGGTPMTAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNAL 78
Cdd:PRK11546    1 MKRNTKiaLVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028197998  79 LTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVPRgagmgyGGCGGGGNHRSGGHMGMGHW 147
Cdd:PRK11546   81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPR------GAGMGYGGCGGGGHMGMGHW 143
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
 3-120 1.73e-17

Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 73.48  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   3 RNNKLALIALSLIALGSTPVLAQNHWGYGDGMqqRGGTPM------TAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYN 76
Cdd:COG3678     2 KLKLLALLLALALALGAASAFAAGPPGGPRGG--RGLRRMleglnlTEEQRQQIRAIRQQYRKQMRALRQQLREAREELR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1028197998  77 ALLTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVP 120
Cdd:COG3678    80 ALLAADKFDEAAVRALADKIAALRAQLAVERAEARNQMYKVLTP 123
Metal_resist pfam13801
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ...
 7-121 7.75e-16

Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.


Pssm-ID: 433488 [Multi-domain]  Cd Length: 119  Bit Score: 68.86  E-value: 7.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028197998   7 LALIALSLIALGSTPVLAQNHWGYG--DGMQQRGGTPMTAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNALLTASSP 84
Cdd:pfam13801   2 LNLFLLGALVGAALRGPGGPPGGGPgrGGMLLRAALGLPAEQRERLRAALRDHARELRALRRELRAARRELAALLAAPPF 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1028197998  85 DTAKINAVAKEMEALNQSLDEQRVKRDVAMAQAGVPR 121
Cdd:pfam13801  82 DPAAIEAALAEARQARAALQAQIEEALLEFAATLSPE 118
CpxP_like cd09916
CpxP component of the bacterial Cpx-two-component system and related proteins; This family ...
 43-116 3.48e-06

CpxP component of the bacterial Cpx-two-component system and related proteins; This family summarizes bacterial proteins related to CpxP, a periplasmic protein that forms part of a two-component system which acts as a global modulator of cell-envelope stress in gram-negative bacteria. CpxP aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to alkaline pH. Functioning as a dimer, it inhibits activation of the kinase CpxA, but also plays a vital role in the quality control system of P pili. It has been suggested that CpxP directly interacts with CpxA via its concave polar surface. Another member of this family, Spy, is also a periplasmic protein that may be involved in the response to stress. The homology between CpxP and Spy suggests similar functions. A characteristic 5-residue sequence motif LTXXQ is found repeated twice in many members of this family.


Pssm-ID: 197366 [Multi-domain]  Cd Length: 96  Bit Score: 42.97  E-value: 3.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028197998  43 TAEQQAAAQKIYDDYYSQTSALRQQLTSKRYEYNALLTASSPDTAKINAVAKEMEALNQSLDEQRVKRDVAMAQ 116
Cdd:cd09916     5 TDEQKAQIKAIRQAARAQMKALREQMRAAREELRALLTADTFDEAAVRALAAEMAELQQELAVERAKARNQIYQ 78
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
44-107 1.45e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.22  E-value: 1.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028197998  44 AEQQAAAQkiyddyYSQTSALRQQLTSKRYEYNALLTASSPDTAKINAVAKEMEALNQSLDEQR 107
Cdd:COG3524   212 PEATAEAL------LQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAER 269
 
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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