{"cross_mech":[],"family":{"alphafold_models":1910,"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":"Bacillithiol (BSH) functions as a general thiol reductant, analogous to glutathione, in a wide range of bacterial species. Bacilliredoxins reduce those proteins that are modified by disulfide bond formation with BSH (S-bacillithiolation) [[cite:PUB00100073]]. This entry represents BrxC from Bacillus subtilis (formerly known as YtxJ) and similar bacterial proteins related to BSH. BrxC is a monothiol bacilliredoxin responsible for the removal of BSH from oxidized cytosolic proteins. It can also debacillithiolate the mixed disulfide form of the bacilliredoxin BrxB [[cite:PUB00055031],[cite:PUB00100075]]. It has a similar fold to thioredoxin. The homologue in Deinococcus radiodurans, named AbxC, plays a role in the response to oxidative stress [[cite:PUB00100126]].","domain_architectures":6,"interpro_id":"IPR022551","known_evidence_count":null,"matches":3076,"name":"Monothiol bacilliredoxin BrxC","partial_evidence_count":null,"pfam_id":"PF11009","proteins":3076,"proteomes":2928,"short_name":"BrxC","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11009","structures":1,"taxa":3744,"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/PF11009.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":1910,"domain_architectures":6,"matches":3076,"proteins":3076,"proteomes":2928,"structures":1,"taxa":3744},"curation_status":"SEEDED","description":"Bacillithiol (BSH) functions as a general thiol reductant, analogous to glutathione, in a wide range of bacterial species. Bacilliredoxins reduce those proteins that are modified by disulfide bond formation with BSH (S-bacillithiolation) [[cite:PUB00100073]]. This entry represents BrxC from Bacillus subtilis (formerly known as YtxJ) and similar bacterial proteins related to BSH. BrxC is a monothiol bacilliredoxin responsible for the removal of BSH from oxidized cytosolic proteins. It can also debacillithiolate the mixed disulfide form of the bacilliredoxin BrxB [[cite:PUB00055031],[cite:PUB00100075]]. It has a similar fold to thioredoxin. The homologue in Deinococcus radiodurans, named AbxC, plays a role in the response to oxidative stress [[cite:PUB00100126]].","id":"Pfam:PF11009","interpro_id":"InterPro:IPR022551","name":"Monothiol bacilliredoxin BrxC","pfam_id":"PF11009","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":"BrxC","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11009"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF11009.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"ed7b4f3e537af2bc17e2a9a7f2d2f90c093cdecc43006b5fc755ca54c5c1df13"}},"protein_examples":{"candidate_count":1,"discovery_scanned":true,"example_count":1,"examples":[{"evidence_scope":"FAMILY_MEMBERSHIP_NOT_FUNCTION","organism":"Bacillus subtilis (strain 168)","origins":[{"cited_uniprot_accession":"","commit":"70edd6f8458845f7d7783ac4f416df519f5e1de6","link_basis":["canonical_example_family_classification"],"mech":"ProteinTraitsMech","path":"data/traits/function/molecular_function/go/translation-elongation-factor-binding-go0061770.yaml","qualification_status":"NOT_ASSESSED","record_id":"GO:0061770","section":"canonical_examples","url":"https://github.com/CultureBotAI/proteintraitsmech/blob/70edd6f8458845f7d7783ac4f416df519f5e1de6/data/traits/function/molecular_function/go/translation-elongation-factor-binding-go0061770.yaml"},{"cited_uniprot_accession":"","commit":"70edd6f8458845f7d7783ac4f416df519f5e1de6","link_basis":["canonical_example_family_classification"],"mech":"ProteinTraitsMech","path":"data/traits/function/protein_family/ncbifam/bacillithiol-system-redox-active-protein-ytxj-tigr04019.yaml","qualification_status":"NOT_ASSESSED","record_id":"NCBIfam:TIGR04019","section":"canonical_examples","url":"https://github.com/CultureBotAI/proteintraitsmech/blob/70edd6f8458845f7d7783ac4f416df519f5e1de6/data/traits/function/protein_family/ncbifam/bacillithiol-system-redox-active-protein-ytxj-tigr04019.yaml"},{"cited_uniprot_accession":"","commit":"70edd6f8458845f7d7783ac4f416df519f5e1de6","link_basis":["canonical_example_family_classification","ptm_own_pfam_record_example"],"mech":"ProteinTraitsMech","path":"data/traits/sequence/family/pfam/brxc-pf11009.yaml","qualification_status":"LEGACY_OR_UNSPECIFIED","record_id":"Pfam:PF11009","section":"canonical_examples","url":"https://github.com/CultureBotAI/proteintraitsmech/blob/70edd6f8458845f7d7783ac4f416df519f5e1de6/data/traits/sequence/family/pfam/brxc-pf11009.yaml"}],"pfam_ids":["PF11009"],"protein_name":"Monothiol bacilliredoxin BrxC","registry_status":"NOT_IN_REGISTRY","reviewed":true,"sequence":"MAKQLIQSEEEFKRIAEQEGVFVFLKHSTTCPISQAAFHEFDAFANQHEDVPAYYLQVQEARPLSNFIAETYGVKHESPQIFIIQNGEVKWHTSHSQITEAAIEQHLS","sequence_length":108,"sequence_origin":"UNIPROT_FETCH","sequence_sha256":"21879052e742384db708fd25d38c748d8b0058c40480e3f007276405485e5b8d","sequence_version":1,"source_url":"https://rest.uniprot.org/uniprotkb/P39914.json","taxon_id":"224308","uniprot_accession":"P39914","uniprot_release":"2026_03"}],"pfam_id":"PF11009","short_name":"BrxC","status":"HAS_SEQUENCE_EXAMPLE","unresolved":[]}}