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Conserved domains on  [gi|1457638235|emb|SVN02984|]
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Uncharacterised protein [Klebsiella pneumoniae]

Protein Classification

YfiR family protein( domain architecture ID 10616153)

YfiR family protein containing a DUF4154 domain, similar to Pseudomonas aeruginosa YfiR, which inhibits the diguanylate cyclase activity of the inner membrane protein YfiN, whereas YfiB in the outer membrane can release this inhibition by sequestration of YfiR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4154 pfam13689
YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. ...
 29-164 1.33e-38

YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. YfiR has been shown to regulate YfiN, a diguanylate cyclase and a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiR may serve as a periplasmic redox sensor that regulates YfiN activity in response to reducing conditions. HmsC in Yersinia Pestis is the orthologue of YfiR from E. coli. HmsC is a periplasmic protein that interacts directly with the periplasmic domain (PD) of HmsD and causes proteolytic degradation of HmsD, which in turn negatively regulates Y. pestis biofilm formation.


:

Pssm-ID: 433405  Cd Length: 140  Bit Score: 128.53  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457638235  29 VRAIVSGIVTYTRWP--SLTGAPKLCIFASSRFTHSLAHEDPDA----LPYQPVIVRNREEAlkTTCDGFYFGSESPTEQ 102
Cdd:pfam13689   1 KAAFLYNFAKFVEWPaeAFATPLRICVLGDDPFGAALDALLAGKtvggRPIRVRRLDDVSEA--SGCHVLYIGRSEAREL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1457638235 103 SELTRRYGPRPLLLIAEQNTDCSIGSAFCLIINDDRVRFSVNLDVLTHSGVRVNPDVLMLAR 164
Cdd:pfam13689  79 AAILAALRGKPVLTVSDGPGFARSGGMINLVRVDGRLRFEINLDAARRAGLKISSKLLRLAR 140
 
Name Accession Description Interval E-value
DUF4154 pfam13689
YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. ...
 29-164 1.33e-38

YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. YfiR has been shown to regulate YfiN, a diguanylate cyclase and a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiR may serve as a periplasmic redox sensor that regulates YfiN activity in response to reducing conditions. HmsC in Yersinia Pestis is the orthologue of YfiR from E. coli. HmsC is a periplasmic protein that interacts directly with the periplasmic domain (PD) of HmsD and causes proteolytic degradation of HmsD, which in turn negatively regulates Y. pestis biofilm formation.


Pssm-ID: 433405  Cd Length: 140  Bit Score: 128.53  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457638235  29 VRAIVSGIVTYTRWP--SLTGAPKLCIFASSRFTHSLAHEDPDA----LPYQPVIVRNREEAlkTTCDGFYFGSESPTEQ 102
Cdd:pfam13689   1 KAAFLYNFAKFVEWPaeAFATPLRICVLGDDPFGAALDALLAGKtvggRPIRVRRLDDVSEA--SGCHVLYIGRSEAREL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1457638235 103 SELTRRYGPRPLLLIAEQNTDCSIGSAFCLIINDDRVRFSVNLDVLTHSGVRVNPDVLMLAR 164
Cdd:pfam13689  79 AAILAALRGKPVLTVSDGPGFARSGGMINLVRVDGRLRFEINLDAARRAGLKISSKLLRLAR 140
 
Name Accession Description Interval E-value
DUF4154 pfam13689
YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. ...
 29-164 1.33e-38

YfiR/HmsC-like; This family of proteins is found in bacteria and includes YfiR from E. coli. YfiR has been shown to regulate YfiN, a diguanylate cyclase and a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiR may serve as a periplasmic redox sensor that regulates YfiN activity in response to reducing conditions. HmsC in Yersinia Pestis is the orthologue of YfiR from E. coli. HmsC is a periplasmic protein that interacts directly with the periplasmic domain (PD) of HmsD and causes proteolytic degradation of HmsD, which in turn negatively regulates Y. pestis biofilm formation.


Pssm-ID: 433405  Cd Length: 140  Bit Score: 128.53  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1457638235  29 VRAIVSGIVTYTRWP--SLTGAPKLCIFASSRFTHSLAHEDPDA----LPYQPVIVRNREEAlkTTCDGFYFGSESPTEQ 102
Cdd:pfam13689   1 KAAFLYNFAKFVEWPaeAFATPLRICVLGDDPFGAALDALLAGKtvggRPIRVRRLDDVSEA--SGCHVLYIGRSEAREL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1457638235 103 SELTRRYGPRPLLLIAEQNTDCSIGSAFCLIINDDRVRFSVNLDVLTHSGVRVNPDVLMLAR 164
Cdd:pfam13689  79 AAILAALRGKPVLTVSDGPGFARSGGMINLVRVDGRLRFEINLDAARRAGLKISSKLLRLAR 140
 
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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