{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O34693","secondaryAccessions":["Q796I2","Q799L3"],"uniProtkbId":"RQCH_BACSU","entryAudit":{"firstPublicDate":"2009-09-22","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":120,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Bacillus subtilis (strain 168)","taxonId":224308,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Bacillaceae","Bacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31155236"}],"value":"Rqc2 homolog RqcH"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31155236"}],"value":"RqcH"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Ribosome-associated protein quality control protein H"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31155236"}],"value":"rqcH"},"synonyms":[{"value":"yloA"}],"orderedLocusNames":[{"value":"BSU15640"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31155236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35264791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38177497"}],"value":"Key component of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation (PubMed:31155236). RqcH recruits Ala-charged tRNA, and with RqcP directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal alanine extensions (Ala tail) (PubMed:31155236, PubMed:35264791, PubMed:38177497). The Ala tail promotes nascent chain degradation (PubMed:31155236). RqcH, RqcP and charged tRNA(Ala) are necessary and sufficient to add an Ala tail to a model stalled nascent peptide; does not add Val (PubMed:34255840). Binds the P-site tRNA in 50S ribosomal subunit, unwinds the anticodon stem and interacts with the splayed anticodon (PubMed:33259811, PubMed:33259810, PubMed:34255840). Selectively binds tRNA(Ala) isoacceptors, even in the absence of the 50S ribosomal subunit (PubMed:31155236, PubMed:33259810, PubMed:34255840). Adds between 1 and at least 8 Ala residues to the nascent chain; detection of the Ala tail requires either deletion of clpP or its inhibition (PubMed:31155236). Binds to 50S ribosomal subunits, at least 30% of which contain a P-site tRNA and thus are obstructed (PubMed:31155236, PubMed:33259811)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31155236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38811035"}],"value":"Associates with isolated or stalled 50S ribosomal subunits (PubMed:31155236, PubMed:33259811, PubMed:33259810, PubMed:34255840). Binds to RqcP (PubMed:33259811, PubMed:33259810, PubMed:34255840). Interacts with ribosomal protein uL11 (PubMed:33259811, PubMed:33259810, PubMed:34255840). Displaced from the 50S subunit by thiostrepton (PubMed:33259810, PubMed:34255840). In crystallized 50S subunits RqcH is variously associated with A/P-site tRNA, P-site tRNA and RqcP, an E-site tRNA or A- and P-site tRNAs and RqcP2(YlmH) (PubMed:33259811, PubMed:33259810, PubMed:34255840, PubMed:38811035)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17586671"}],"value":"Highly expressed during stationary phase (PubMed:17586671)"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17586671"}],"value":"Up-regulated under secretion stress conditions, possibly in a CssR/CssS-dependent manner (PubMed:17586671)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"}],"value":"Has 4 domains; N-terminal NFACT-N, central helix-hairpin-helix (HhH), 2 coiled coil domains with a beta-hairpin in the middle (CC-M), and C-terminal NFACT-R (PubMed:33259811, PubMed:33259810, PubMed:34255840). The NFACT-N domain contacts 23S rRNA, the A/P-site tRNA anticodon and recognizes tRNA(Ala), while the M beta hairpin binds protein uL11 near the base of the bL12 stalk (PubMed:33259810, PubMed:34255840)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31155236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35264791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38177497"}],"value":"Not essential in rich media; synthetic growth defects are seen in double rqcH-ssrA mutants, further exacerbated by translational inhibitors spectinomycin and erythromycin or at elevated temperatures (PubMed:31155236, PubMed:33259811). Decreased accumulation of a stalled reporter protein (PubMed:31155236). Double rqcH-rqcP deletion strains grow normally in rich media (PubMed:33259811). Triple rqcH-clpP-ssrA mutants cannot be generated (PubMed:31155236). No change in sensitivity to erythromycin; double mutSB-rqcH and triple mutSB-rqcH-ssrA deletion strains are hypersensitive to erythromycin (PubMed:35264791). Loss of Ala tailing (PubMed:38177497)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31155236"}],"value":"Activity of this protein is best tested in a clpP or ssrA deletion mutant; ssrA (tmRNA) encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, which targets the nascent protein for degradation"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00844"}],"value":"Belongs to the NEMF family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA04416.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31155236"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA74268.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31155236"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAB13438.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31155236"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"Rqc2 homolog RqcH","featureId":"PRO_0000383595"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"NFACT-N domain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"}]},{"type":"Region","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"HhH domain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"}]},{"type":"Region","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Coiled-coil-M (CCM)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"}]},{"type":"Region","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"NFACT-R","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"}]},{"type":"Coiled coil","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AQC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AQD"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AS8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AS9"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7ASA"}]},{"type":"Coiled coil","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33259811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34255840"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AQC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AQD"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AS8"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7AS9"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7ASA"}]},{"type":"Mutagenesis","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Still interacts with 50S ribosomal subunit. 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