Hemolysin coregulated protein Hcp (TssD); T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. These tube and trans-envelope sub-assemblies are linked via TssK. This entry comprises family members such as the inner tube protein Hcp (TssD). Hcp proteins form hexamers that stack to form the inner tube/needle structure of the puncturing device. Other functions have also been described for Hcp proteins, for example, some Hcp proteins have been shown to have a chaperone function in that they bind to and stabilize effectors. In addition, there are 'evolved' Hcp proteins that have the Hcp domain at the N-terminal half of the protein and a toxic effector function present in the C-terminal portion of the protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2446347203   2 AFKARLNFSGKEYDVLNCSYALNRDVDSKGRPSSGVYGGTIDIEVESTEDTSIIEAMVNnQYKPVTGTLLIKKSEEDAKM 81
Cdd:pfam17642   1 SFKAKLRIDGKEYNVLDCNYSFNQETDSKGRPQSEVRGGTITVTIESTPDTELLEWMLN-PFKRKDGSIVFYKRDEDSKL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2446347203  82 KELSFEDGYIVKYSEGLDITGETPMSYKFTISARKLKLGNAEHVNDWP 129
Cdd:pfam17642  80 KKIEFENAYCVGYNENFDATGSNPMTTTLTISAKKIKLGGAEHENNWP 127

Hemolysin coregulated protein Hcp (TssD); T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. These tube and trans-envelope sub-assemblies are linked via TssK. This entry comprises family members such as the inner tube protein Hcp (TssD). Hcp proteins form hexamers that stack to form the inner tube/needle structure of the puncturing device. Other functions have also been described for Hcp proteins, for example, some Hcp proteins have been shown to have a chaperone function in that they bind to and stabilize effectors. In addition, there are 'evolved' Hcp proteins that have the Hcp domain at the N-terminal half of the protein and a toxic effector function present in the C-terminal portion of the protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2446347203   2 AFKARLNFSGKEYDVLNCSYALNRDVDSKGRPSSGVYGGTIDIEVESTEDTSIIEAMVNnQYKPVTGTLLIKKSEEDAKM 81
Cdd:pfam17642   1 SFKAKLRIDGKEYNVLDCNYSFNQETDSKGRPQSEVRGGTITVTIESTPDTELLEWMLN-PFKRKDGSIVFYKRDEDSKL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2446347203  82 KELSFEDGYIVKYSEGLDITGETPMSYKFTISARKLKLGNAEHVNDWP 129
Cdd:pfam17642  80 KKIEFENAYCVGYNENFDATGSNPMTTTLTISAKKIKLGGAEHENNWP 127

Hemolysin coregulated protein Hcp (TssD); T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. These tube and trans-envelope sub-assemblies are linked via TssK. This entry comprises family members such as the inner tube protein Hcp (TssD). Hcp proteins form hexamers that stack to form the inner tube/needle structure of the puncturing device. Other functions have also been described for Hcp proteins, for example, some Hcp proteins have been shown to have a chaperone function in that they bind to and stabilize effectors. In addition, there are 'evolved' Hcp proteins that have the Hcp domain at the N-terminal half of the protein and a toxic effector function present in the C-terminal portion of the protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2446347203   2 AFKARLNFSGKEYDVLNCSYALNRDVDSKGRPSSGVYGGTIDIEVESTEDTSIIEAMVNnQYKPVTGTLLIKKSEEDAKM 81
Cdd:pfam17642   1 SFKAKLRIDGKEYNVLDCNYSFNQETDSKGRPQSEVRGGTITVTIESTPDTELLEWMLN-PFKRKDGSIVFYKRDEDSKL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2446347203  82 KELSFEDGYIVKYSEGLDITGETPMSYKFTISARKLKLGNAEHVNDWP 129
Cdd:pfam17642  80 KKIEFENAYCVGYNENFDATGSNPMTTTLTISAKKIKLGGAEHENNWP 127