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Database: UniProt
Entry: K6DE86_9BACI
LinkDB: K6DE86_9BACI
Original site: K6DE86_9BACI 
ID   K6DE86_9BACI            Unreviewed;       570 AA.
AC   K6DE86;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   18-JUN-2025, entry version 34.
DE   RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE            Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN   Name=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN   ORFNames=BABA_16532 {ECO:0000313|EMBL:EKN66373.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN66373.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN66373.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- FUNCTION: Key component of the ribosome quality control system (RQC), a
CC       ribosome-associated complex that mediates the extraction of
CC       incompletely synthesized nascent chains from stalled ribosomes and
CC       their subsequent degradation. RqcH recruits Ala-charged tRNA, and with
CC       RqcP directs the elongation of stalled nascent chains on 50S ribosomal
CC       subunits, leading to non-templated C-terminal alanine extensions (Ala
CC       tail). The Ala tail promotes nascent chain degradation. May add between
CC       1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00844}.
CC   -!- SUBUNIT: Associates with stalled 50S ribosomal subunits. Binds to RqcP.
CC       {ECO:0000256|HAMAP-Rule:MF_00844}.
CC   -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00844}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKN66373.1}.
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DR   EMBL; AJLS01000118; EKN66373.1; -; Genomic_DNA.
DR   RefSeq; WP_007086302.1; NZ_AJLS01000118.1.
DR   AlphaFoldDB; K6DE86; -.
DR   STRING; 1117379.BABA_16532; -.
DR   PATRIC; fig|1117379.3.peg.3434; -.
DR   eggNOG; COG1293; Bacteria.
DR   OrthoDB; 9766163at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:1990112; C:RQC complex; IEA:TreeGrafter.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR   FunFam; 2.30.310.10:FF:000004; Fibronectin-binding protein A; 1.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 3.40.970.40; fibrinogen binding protein from staphylococcus aureus domain like; 1.
DR   Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR   HAMAP; MF_00844_B; RqcH_B; 1.
DR   InterPro; IPR051608; RQC_Subunit_NEMF.
DR   InterPro; IPR043682; RqcH_bacterial.
DR   PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR   Pfam; PF18297; NFACT-R_2; 1.
DR   Pfam; PF05833; NFACT_N; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00844};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00844};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00844}.
SQ   SEQUENCE   570 AA;  64848 MW;  A76A4FEDCD127C6D CRC64;
     MSFDGLFTKA MVDELVRSLK GGRINKVHQP YKNEVILTIR ANGVNQKLLL SAHPSYARVQ
     LTNESYDNPS EPPMFCMLLR KHIEGHILED LYQVENDRMI IFEIKGRNEI GDISNKQLII
     EIMGRHSNIV IVDKTRNVIL DSIKHVSFAV NSHRAILPGQ PYIFPPAQNK INPYEAVEED
     VVKTVDFIGG KLDRQLVEHF AGTSPLFAKE VIFQSGLANR TTVPGTFIRL IKKIADGDIS
     PSIISANGKD SFYLFPLEHL QGEIKTFPTL SELLDRFYFG KAERDRVKQQ GNDIERFISN
     EKDKNEKKIR KLEDTLKEAE RAEQFQRYGE LLTANLYSAK KGMKEIEVLD YYDELGGTIV
     IPLDPRKTPS ENAQKYFSKY QKAKNAVAVV VEQIEKAHLE VVYFDNLLQQ VLAASPKDIQ
     EIREELIDGG YIRERKKRSG KKTQNIKPVL DHFIASDGTD IIVGKNNKQN DYLTNKLAAR
     DEIWLHTKDI PGSHVVIRSK EPSDETIKEA AVLAAYYSKA RNSSSVPVDF TKVRYVKKPS
     GAKPGFVIYD NQQTVYITPD EEIVLKLKKK
//
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