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{
    "metadata": {
        "accession": "PF18883",
        "entry_id": null,
        "type": "repeat",
        "go_terms": null,
        "source_database": "pfam",
        "member_databases": null,
        "integrated": "IPR043990",
        "hierarchy": null,
        "name": {
            "name": "Autochaperone Domain Type 1",
            "short": "AC_1"
        },
        "description": [
            {
                "text": "<p>This entry represents the autochaperone domain of type 1 (AC-1) in the Type Va Secretion System (T5aSS). Autotransporters (ATs) belong to a family of modular proteins secreted by the Type V, subtype a, secretion system (T5aSS) and considered as an important source of virulence factors in lipopolysaccharidic diderm bacteria (archetypical Gram-negative bacteria). The AC of type 1 with beta-fold appears as a prevalent and conserved structural element exclusively associated to beta-helical AT passenger [[cite:PUB00094659]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00094659": {
                "PMID": 29375499,
                "ISBN": null,
                "volume": "8",
                "issue": null,
                "year": 2017,
                "title": "Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a β-Helical Passenger.",
                "URL": null,
                "raw_pages": "2607",
                "medline_journal": "Front Microbiol",
                "ISO_journal": "Front Microbiol",
                "authors": [
                    "Rojas-Lopez M",
                    "Zorgani MA",
                    "Kelley LA",
                    "Bailly X",
                    "Kajava AV",
                    "Henderson IR",
                    "Polticelli F",
                    "Pizza M",
                    "Rosini R",
                    "Desvaux M."
                ],
                "DOI_URL": null
            }
        },
        "set_info": {
            "accession": "CL0268",
            "name": "Pec_lyase-like"
        },
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 176,
            "interactions": 0,
            "matches": 9031,
            "pathways": 0,
            "proteins": 9008,
            "proteomes": 1229,
            "sets": 1,
            "structural_models": {
                "alphafold": 5655,
                "bfvd": 0
            },
            "structures": 5,
            "taxa": 2521
        },
        "entry_annotations": {
            "hmm": 0,
            "logo": 0,
            "alignment:seed": 15,
            "alignment:full": 859
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "3ml3",
            "name": "Crystal structure of the IcsA autochaperone region"
        }
    }
}