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Conserved domains on  [gi|517178321|ref|WP_018367139|]
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ImmA/IrrE family metallo-endopeptidase [Streptococcus didelphis]

Protein Classification

ImmA/IrrE family metallo-endopeptidase( domain architecture ID 10006736)

ImmA/IrrE family metallo-endopeptidase similar to Bacillus subtilis metallopeptidase ImmA, which is involved in the regulation of horizontal gene transfer through the integrative and conjugative element ICEBs1

PubMed:  18761623

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 75-158 9.78e-18

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442104  Cd Length: 105  Bit Score: 76.62  E-value: 9.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517178321  75 PISRQNFTKCHELGHILLkHKGNIFLESKDNKNQVEIEADIFSASILMPDILLIDFIYYKK-KHFQDIFKLLNVSAEALN 153
Cdd:COG2856    8 SPERQRFTLAHELGHLLL-HRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLsEDLEELAKRFGVSEEALL 86


                 ....*
gi 517178321 154 IRLIE 158
Cdd:COG2856   87 YRLKE 91
 
Name Accession Description Interval E-value
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 75-158 9.78e-18

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442104  Cd Length: 105  Bit Score: 76.62  E-value: 9.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517178321  75 PISRQNFTKCHELGHILLkHKGNIFLESKDNKNQVEIEADIFSASILMPDILLIDFIYYKK-KHFQDIFKLLNVSAEALN 153
Cdd:COG2856    8 SPERQRFTLAHELGHLLL-HRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLsEDLEELAKRFGVSEEALL 86


                 ....*
gi 517178321 154 IRLIE 158
Cdd:COG2856   87 YRLKE 91
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 43-156 1.01e-13

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 66.29  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517178321   43 IKISPLHFTKSNISGMTITNSKGTsLHYEKVNPISRQNFTKCHELGHILLKHKGNIFLESKDNKN--QVEIEADIFSASI 120
Cdd:pfam06114   6 IRVFFLPLGAEDGDGRRFDRHTPV-IFLNENLSPTRQRFTLAHELGHLLLHEGGDTLSDQFDFKTaeAREREANIFAAAL 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517178321  121 LMPDILLIDFIY-YKKKHFQDIFKLLNVSAEALNIRL 156
Cdd:pfam06114  85 LMPYEAFLAAAEtLRYDLELLLAERFGVSYEAVAHRL 121
 
Name Accession Description Interval E-value
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 75-158 9.78e-18

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442104  Cd Length: 105  Bit Score: 76.62  E-value: 9.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517178321  75 PISRQNFTKCHELGHILLkHKGNIFLESKDNKNQVEIEADIFSASILMPDILLIDFIYYKK-KHFQDIFKLLNVSAEALN 153
Cdd:COG2856    8 SPERQRFTLAHELGHLLL-HRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLsEDLEELAKRFGVSEEALL 86


                 ....*
gi 517178321 154 IRLIE 158
Cdd:COG2856   87 YRLKE 91
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 43-156 1.01e-13

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 66.29  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517178321   43 IKISPLHFTKSNISGMTITNSKGTsLHYEKVNPISRQNFTKCHELGHILLKHKGNIFLESKDNKN--QVEIEADIFSASI 120
Cdd:pfam06114   6 IRVFFLPLGAEDGDGRRFDRHTPV-IFLNENLSPTRQRFTLAHELGHLLLHEGGDTLSDQFDFKTaeAREREANIFAAAL 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517178321  121 LMPDILLIDFIY-YKKKHFQDIFKLLNVSAEALNIRL 156
Cdd:pfam06114  85 LMPYEAFLAAAEtLRYDLELLLAERFGVSYEAVAHRL 121
 
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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