proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat superfamily, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. The PAAR-repeat proteins form a diverse superfamily with several subgroups extended both N- and C-terminally by domains with various predicted functions; the termini are exposed to solution, and do not distort the VgrG binding site. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544   3 RPAARISDSVAHPLPpvLTGGPGSRNVLIGNLPAWRGipaapvagllaakqatdatiisveaaskaalgtpaapaaiate 82
Cdd:cd14741     1 PPAARIGDSTAHGGP--LTPGPGSPNVLIGGFPAWRA------------------------------------------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544  83 qstktsllasmnssirasalGADIHVCTTPLPVPPHGSGVVIDGSKTVLINGLPACRMGDTIVEAiGPINKITRGCNSVL 162
Cdd:cd14741    36 --------------------GGDGHVCPLVTGPVPHVGGVVAAGSTTVLINGLPAARMGDMIVEG-GPPNTIAMGAPTVL 94

                  .
gi 1836863544 163 I 163
Cdd:cd14741    95 I 95

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family in bacteria as well as some archaea, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544   3 RPAARISDSVAHPLPpvLTGGPGSRNVLIGNLPAWRGipaapvagllaakqatdatiisveaaskaalgtpaapaaiate 82
Cdd:cd14741     1 PPAARIGDSTAHGGP--LTPGPGSPNVLIGGFPAWRA------------------------------------------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544  83 qstktsllasmnssirasalGADIHVCTTPLPVPPHGSGVVIDGSKTVLINGLPACRMGDTIVEAiGPINKITRGCNSVL 162
Cdd:cd14741    36 --------------------GGDGHVCPLVTGPVPHVGGVVAAGSTTVLINGLPAARMGDMIVEG-GPPNTIAMGAPTVL 94

                  .
gi 1836863544 163 I 163
Cdd:cd14741    95 I 95

PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. It is also found as a triplet of tandem repeats comprising the entire length in a another family of hypothetical proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1836863544 116 PPHGSGVVIDGSKTVLINGLPACRMGDTIVEAI-GPINKITRGCNSVLIGG 165
Cdd:pfam05488   4 KTSHGGVVITGSPTVLIGGKPAARVGDLVVCPPcGGGGPIAEGSPTVLING 54

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family in bacteria as well as some archaea, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544   3 RPAARISDSVAHPLPpvLTGGPGSRNVLIGNLPAWRGipaapvagllaakqatdatiisveaaskaalgtpaapaaiate 82
Cdd:cd14741     1 PPAARIGDSTAHGGP--LTPGPGSPNVLIGGFPAWRA------------------------------------------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836863544  83 qstktsllasmnssirasalGADIHVCTTPLPVPPHGSGVVIDGSKTVLINGLPACRMGDTIVEAiGPINKITRGCNSVL 162
Cdd:cd14741    36 --------------------GGDGHVCPLVTGPVPHVGGVVAAGSTTVLINGLPAARMGDMIVEG-GPPNTIAMGAPTVL 94

                  .
gi 1836863544 163 I 163
Cdd:cd14741    95 I 95

Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular trafficking, secretion, and vesicular transport];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1836863544 116 PPHGSGVVIDGSKTVLINGLPACRMGDTIVEAIGPINKITRGCNSVLIGG 165
Cdd:COG4104    11 KTSHGGPVISGSPTVLIGGRPAARVGDKVSCPKHGPDTIAEGSPTVLING 60

PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. It is also found as a triplet of tandem repeats comprising the entire length in a another family of hypothetical proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1836863544 116 PPHGSGVVIDGSKTVLINGLPACRMGDTIVEAI-GPINKITRGCNSVLIGG 165
Cdd:pfam05488   4 KTSHGGVVITGSPTVLIGGKPAARVGDLVVCPPcGGGGPIAEGSPTVLING 54

proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat superfamily, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. The PAAR-repeat proteins form a diverse superfamily with several subgroups extended both N- and C-terminally by domains with various predicted functions; the termini are exposed to solution, and do not distort the VgrG binding site. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1836863544 121 GVVIDGSKTVLINGLPACRMGDtIVEAIGPINKITRGCNSVLIGG 165
Cdd:cd14671    15 GPVISGSPNVFINGRPAARVGD-VGDHPGGGNAIVSGSGTVFING 58

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1836863544 114 PVPPHGSGVVIDGSKTVLINGLPACRMGDTIveaigpinkitrGCNSVLIGG 165
Cdd:cd14737    48 PKHPPHGGVIASGSSTVFINGKPAARVGDPV------------SCGGTVAGG 87

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of bacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). A few members contains C-terminal domain extensions corresponding to Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences as well as uncharacterized domains such as DUF4150. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1836863544 111 TPLPVPPHGSGVVIDGSKTVLINGLPACRMGD 142
Cdd:cd14740    67 GGPSVPPANPGTIVMGSSTVFINGKPAARMGD 98

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1836863544 122 VVIDGSKTVLINGLPACRMGDTIveAIGpiNKITRGCNSVLIG 164
Cdd:cd14738    56 TIVQGSSTVLIGGKPAARMGDST--AHG--GVIVSGVPTVLIG 94