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Conserved domains on  [gi|491008808|ref|WP_004870523|]
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MULTISPECIES: zinc resistance sensor/chaperone ZraP [Klebsiella]

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;
1-140 1.14e-68

zinc resistance sensor/chaperone ZraP;


:

Pssm-ID: 183189  Cd Length: 143  Bit Score: 203.54  E-value: 1.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808   1 MKRNKKMTLTLIALAALTFGSSSAWARHHWNNGNGMGPQGYNQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNAL 80
Cdd:PRK11546   1 MKRNTKIALVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491008808  81 LTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIPRGEGMGCGGRG---HMGMNHW 140
Cdd:PRK11546  81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPRGAGMGYGGCGgggHMGMGHW 143
 
Name Accession Description Interval E-value
zraP PRK11546
zinc resistance sensor/chaperone ZraP;
1-140 1.14e-68

zinc resistance sensor/chaperone ZraP;


Pssm-ID: 183189  Cd Length: 143  Bit Score: 203.54  E-value: 1.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808   1 MKRNKKMTLTLIALAALTFGSSSAWARHHWNNGNGMGPQGYNQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNAL 80
Cdd:PRK11546   1 MKRNTKIALVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491008808  81 LTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIPRGEGMGCGGRG---HMGMNHW 140
Cdd:PRK11546  81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPRGAGMGYGGCGgggHMGMGHW 143
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
 5-122 3.12e-19

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


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 77.71  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808   5 KKMTLTLIALAALTFGSSSAWARHHWNNGNGMGPQGY----NQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNAL 80
Cdd:COG3678    2 KLKLLALLLALALALGAASAFAAGPPGGPRGGRGLRRmlegLNLTEEQRQQIRAIRQQYRKQMRALRQQLREAREELRAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491008808  81 LTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIP 122
Cdd:COG3678   82 LAADKFDEAAVRALADKIAALRAQLAVERAEARNQMYKVLTP 123
Metal_resist pfam13801
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ...
 8-123 4.05e-18

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: 74.25  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808    8 TLTLIALAALTFGSSSAWARHHWNNGN--GMGPQGYNQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNALLTTDK 85
Cdd:pfam13801   1 ALNLFLLGALVGAALRGPGGPPGGGPGrgGMLLRAALGLPAEQRERLRAALRDHARELRALRRELRAARRELAALLAAPP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491008808   86 PDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIPR 123
Cdd:pfam13801  81 FDPAAIEAALAEARQARAALQAQIEEALLEFAATLSPE 118
CpxP_like cd09916
CpxP component of the bacterial Cpx-two-component system and related proteins; This family ...
 43-118 3.30e-07

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: 45.28  E-value: 3.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491008808  43 QLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNALLTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQ 118
Cdd:cd09916    3 DLTDEQKAQIKAIRQAARAQMKALREQMRAAREELRALLTADTFDEAAVRALAAEMAELQQELAVERAKARNQIYQ 78
 
Name Accession Description Interval E-value
zraP PRK11546
zinc resistance sensor/chaperone ZraP;
1-140 1.14e-68

zinc resistance sensor/chaperone ZraP;


Pssm-ID: 183189  Cd Length: 143  Bit Score: 203.54  E-value: 1.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808   1 MKRNKKMTLTLIALAALTFGSSSAWARHHWNNGNGMGPQGYNQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNAL 80
Cdd:PRK11546   1 MKRNTKIALVLMALSALAMGSGSAFAHHHWGGGHGMWQQNAAPLTTEQQAAWQKIHNDFYAQTSALRQQLVSKRYEYNAL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491008808  81 LTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIPRGEGMGCGGRG---HMGMNHW 140
Cdd:PRK11546  81 LTANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPRGAGMGYGGCGgggHMGMGHW 143
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
 5-122 3.12e-19

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


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 77.71  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808   5 KKMTLTLIALAALTFGSSSAWARHHWNNGNGMGPQGY----NQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNAL 80
Cdd:COG3678    2 KLKLLALLLALALALGAASAFAAGPPGGPRGGRGLRRmlegLNLTEEQRQQIRAIRQQYRKQMRALRQQLREAREELRAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491008808  81 LTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIP 122
Cdd:COG3678   82 LAADKFDEAAVRALADKIAALRAQLAVERAEARNQMYKVLTP 123
Metal_resist pfam13801
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ...
 8-123 4.05e-18

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: 74.25  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491008808    8 TLTLIALAALTFGSSSAWARHHWNNGN--GMGPQGYNQLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNALLTTDK 85
Cdd:pfam13801   1 ALNLFLLGALVGAALRGPGGPPGGGPGrgGMLLRAALGLPAEQRERLRAALRDHARELRALRRELRAARRELAALLAAPP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491008808   86 PDSAKIESVAQEMDALGQKLAQQRVKFDLALAQAGIPR 123
Cdd:pfam13801  81 FDPAAIEAALAEARQARAALQAQIEEALLEFAATLSPE 118
CpxP_like cd09916
CpxP component of the bacterial Cpx-two-component system and related proteins; This family ...
 43-118 3.30e-07

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: 45.28  E-value: 3.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491008808  43 QLTTEQQATAQKLHNDFYEQTRVLRQQLISKRYEYNALLTTDKPDSAKIESVAQEMDALGQKLAQQRVKFDLALAQ 118
Cdd:cd09916    3 DLTDEQKAQIKAIRQAARAQMKALREQMRAAREELRALLTADTFDEAAVRALAAEMAELQQELAVERAKARNQIYQ 78
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
66-112 1.99e-04

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 39.83  E-value: 1.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 491008808  66 LRQQLISKRYEYNALLTTDKPDSAKIESVAQEMDALGQKLAQQRVKF 112
Cdd:COG3524  226 LEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARL 272
 
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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