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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740903   24 AEKLNIQVEWCDFGAMPLGKNAYDNQEPIILLNNSikHTPTQY-FILGHELGHVIFHEGLIGYYTSVKHGH-SKFEREAD 101
Cdd:pfam06114   1 AERLGIRVFFLPLGAEDGDGRRFDRHTPVIFLNEN--LSPTRQrFTLAHELGHLLLHEGGDTLSDQFDFKTaEAREREAN 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489740903  102 EFSVGLM---GMLFIEENGHIPYSYRELSYQYGVPF 134
Cdd:pfam06114  79 IFAAALLmpyEAFLAAAETLRYDLELLLAERFGVSY 114

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740903   24 AEKLNIQVEWCDFGAMPLGKNAYDNQEPIILLNNSikHTPTQY-FILGHELGHVIFHEGLIGYYTSVKHGH-SKFEREAD 101
Cdd:pfam06114   1 AERLGIRVFFLPLGAEDGDGRRFDRHTPVIFLNEN--LSPTRQrFTLAHELGHLLLHEGGDTLSDQFDFKTaEAREREAN 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489740903  102 EFSVGLM---GMLFIEENGHIPYSYRELSYQYGVPF 134
Cdd:pfam06114  79 IFAAALLmpyEAFLAAAETLRYDLELLLAERFGVSY 114

Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489740903  67 FILGHELGHVIFHEGLIGYYTsvkhgHSK-FEREADEFSVGLM 108
Cdd:cd07324   58 AVLAHEIGHVTLRHIARQLER-----YSRdQEREADRLGLQLL 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740903   24 AEKLNIQVEWCDFGAMPLGKNAYDNQEPIILLNNSikHTPTQY-FILGHELGHVIFHEGLIGYYTSVKHGH-SKFEREAD 101
Cdd:pfam06114   1 AERLGIRVFFLPLGAEDGDGRRFDRHTPVIFLNEN--LSPTRQrFTLAHELGHLLLHEGGDTLSDQFDFKTaEAREREAN 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489740903  102 EFSVGLM---GMLFIEENGHIPYSYRELSYQYGVPF 134
Cdd:pfam06114  79 IFAAALLmpyEAFLAAAETLRYDLELLLAERFGVSY 114

Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489740903  67 FILGHELGHVIFHEGLIGYYTsvkhgHSK-FEREADEFSVGLM 108
Cdd:cd07324   58 AVLAHEIGHVTLRHIARQLER-----YSRdQEREADRLGLQLL 95