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{
    "metadata": {
        "accession": "IPR000802",
        "entry_id": null,
        "type": "family",
        "go_terms": [
            {
                "identifier": "GO:0015105",
                "name": "arsenite transmembrane transporter activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0015700",
                "name": "arsenite transport",
                "category": {
                    "code": "P",
                    "name": "biological_process"
                }
            },
            {
                "identifier": "GO:0016020",
                "name": "membrane",
                "category": {
                    "code": "C",
                    "name": "cellular_component"
                }
            }
        ],
        "source_database": "interpro",
        "member_databases": {
            "cdd": {
                "cd01118": "ArsB_permease"
            },
            "prints": {
                "PR00758": "ARSENICPUMP"
            },
            "ncbifam": {
                "TIGR00935": "arsenite/antimonite efflux transporter"
            },
            "pfam": {
                "PF02040": "Arsenical pump membrane protein"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR000802",
            "name": "Arsenical pump membrane protein, ArsB",
            "type": "Family",
            "children": []
        },
        "name": {
            "name": "Arsenical pump membrane protein, ArsB",
            "short": "Arsenical_pump_ArsB"
        },
        "description": [
            {
                "text": "<p>Arsenic is a toxic metalloid whose trivalent and pentavalent ions inhibit a variety of biochemical processes. Operons that encode arsenic resistance have been found in multicopy plasmids from both Gram-positive and Gram-negative bacteria [[cite:PUB00002267]]. The resistance mechanism is encoded from a single operon, which houses an anion pump. The pump has two polypeptide components: a catalytic subunit (the ArsA protein), which functions as an oxyanion-stimulated ATPase; and an arsenite export component (the ArsB protein), which is associated with the inner membrane [[cite:PUB00002587]]. The ArsA and ArsB proteins are thought to form a membrane complex that functions as an anion-translocating ATPase.</p>\n\n<p>The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00002267": {
                "PMID": 7721697,
                "ISBN": null,
                "volume": "177",
                "issue": "8",
                "year": 1995,
                "title": "An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria.",
                "URL": null,
                "raw_pages": "2050-6",
                "medline_journal": "J Bacteriol",
                "ISO_journal": "J. Bacteriol.",
                "authors": [
                    "Diorio C",
                    "Cai J",
                    "Marmor J",
                    "Shinder R",
                    "DuBow MS."
                ],
                "DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7721697&action=stream&blobtype=pdf"
            },
            "PUB00002587": {
                "PMID": 1688427,
                "ISBN": null,
                "volume": "265",
                "issue": "1",
                "year": 1990,
                "title": "Molecular characterization of an anion pump. The ArsB protein is the membrane anchor for the ArsA protein.",
                "URL": null,
                "raw_pages": "190-4",
                "medline_journal": "J Biol Chem",
                "ISO_journal": "J. Biol. Chem.",
                "authors": [
                    "Tisa LS",
                    "Rosen BP."
                ],
                "DOI_URL": "http://intl.jbc.org/cgi/reprint/265/1/190.pdf"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 18,
            "interactions": 0,
            "matches": 40821,
            "pathways": 0,
            "proteins": 16075,
            "proteomes": 7397,
            "sets": 0,
            "structural_models": {
                "alphafold": 12082,
                "bfvd": 0
            },
            "structures": 0,
            "taxa": 13502
        },
        "entry_annotations": {
            "alignment:seed": 1,
            "alignment:full": 1713
        },
        "cross_references": {
            "gp": {
                "displayName": "Genome Properties",
                "description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
                "rank": 45,
                "accessions": [
                    {
                        "accession": "GenProp0474",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0474"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}