{"cross_mech":[],"family":{"alphafold_models":3141,"candidate_reasons":["pfam_previous_unknown_name"],"characterization_status":"","context_evidence_count":null,"cross_mech":{"example_proteins":0,"protein_traits_record":false,"records_by_mech":{},"scanned":false},"curation_status":"SEEDED","demotion_reasons":[],"description":"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 [[cite:PUB00090998]]. VipA is a family of Gram-negative bacterial proteins that form part of the type VI pathogenic secretion system. Members have been variously defined as VC_A0107 family, Hcp2, TssB and VipA, for ClpV-interacting proteins. VipB and VipA proteins interact very closely to form the shaft of the pathogenic penetrating needle system [[cite:PUB00075705],[cite:PUB00075433],[cite:PUB00075706]]. VipA and VipB (TssB and TssC) proteins were shown to form a cog-wheel like tubular structure in V. cholerae that was noticed to resemble T4 phage gp18 polysheath. Two beta-strands of VipA and four beta-strands of VipB intertwine forming the middle layer of the sheath. The sheath assembles around an inner Hcp tube and is attached to a structure called a baseplate that spans the bacterial membranes. Importantly, VipA/VipB sheath was shown to form a long contractile organelle in V. cholerae and in E. coli, suggesting that sheath contraction powers the secretion [[cite:PUB00091000]].","domain_architectures":12,"interpro_id":"IPR008312","known_evidence_count":null,"matches":5021,"name":"Type VI secretion system, VipA, VC_A0107 or Hcp2","partial_evidence_count":null,"pfam_id":"PF05591","proteins":4990,"proteomes":3299,"short_name":"T6SS_VipA","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05591","structures":11,"taxa":4768,"unknown_status":"EX_DUF"},"inputs":{"cross_mech":"cross-mech-duf-examples-2026-10-10","members":"pfam-uniprot-uniref90-2026-10-07","protein_examples":"duf-protein-examples-2026-10-13","worklist":"interpro-pfam-duf-2026-10-10"},"members":[],"metadata":{"curation_status":"SEEDED","local_source":"source/data/families/PF05591.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":3141,"domain_architectures":12,"matches":5021,"proteins":4990,"proteomes":3299,"structures":11,"taxa":4768},"curation_status":"SEEDED","description":"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 [[cite:PUB00090998]]. VipA is a family of Gram-negative bacterial proteins that form part of the type VI pathogenic secretion system. Members have been variously defined as VC_A0107 family, Hcp2, TssB and VipA, for ClpV-interacting proteins. VipB and VipA proteins interact very closely to form the shaft of the pathogenic penetrating needle system [[cite:PUB00075705],[cite:PUB00075433],[cite:PUB00075706]]. VipA and VipB (TssB and TssC) proteins were shown to form a cog-wheel like tubular structure in V. cholerae that was noticed to resemble T4 phage gp18 polysheath. Two beta-strands of VipA and four beta-strands of VipB intertwine forming the middle layer of the sheath. The sheath assembles around an inner Hcp tube and is attached to a structure called a baseplate that spans the bacterial membranes. Importantly, VipA/VipB sheath was shown to form a long contractile organelle in V. cholerae and in E. coli, suggesting that sheath contraction powers the secretion [[cite:PUB00091000]].","id":"Pfam:PF05591","interpro_id":"InterPro:IPR008312","name":"Type VI secretion system, VipA, VC_A0107 or Hcp2","pfam_id":"PF05591","provenance":{"generated_at":"2026-10-10T07:44:21.614711Z","path":"data/worklists/interpro-pfam-duf-2026-10-10.json","sha256":"17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383","snapshot_id":"interpro-pfam-duf-2026-10-10","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/"},"seed_status":"EX_DUF","short_name":"T6SS_VipA","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05591"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF05591.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"6f4d8f838f11ef6fdf2d778c6bdba8683c01049ea915ce6b14c9c3f28dfd8257"}},"protein_examples":{"candidate_count":0,"discovery_scanned":true,"example_count":0,"examples":[],"pfam_id":"PF05591","short_name":"T6SS_VipA","status":"NO_SIBLING_CANDIDATE","unresolved":[]}}
