ID D2BRB3_LACLK Unreviewed; 540 AA.
AC D2BRB3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=yngB {ECO:0000313|EMBL:ADA65088.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN OrderedLocusNames=LLKF_1417 {ECO:0000313|EMBL:ADA65088.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA65088.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ADA65088.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ADA65088.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
CC -!- FUNCTION: Part of the ribosome quality control system (RQC). Recruits
CC Ala-charged tRNA and directs the elongation of stalled nascent chains
CC on 50S ribosomal subunits, leading to non-templated C-terminal Ala
CC extensions (Ala tail). The Ala tail promotes nascent chain degradation.
CC May add between 1 and at least 8 Ala residues. Binds to stalled 50S
CC ribosomal subunits. {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000256|HAMAP-
CC Rule:MF_00844}.
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DR EMBL; CP001834; ADA65088.1; -; Genomic_DNA.
DR RefSeq; WP_012897952.1; NC_013656.1.
DR AlphaFoldDB; D2BRB3; -.
DR KEGG; llk:LLKF_1417; -.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000001886; Chromosome.
DR GO; GO:0043023; F:ribosomal large subunit 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 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; IPR008532; NFACT_RNA-bd.
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; PF05670; NFACT-R_1; 1.
DR Pfam; PF18297; NFACT-R_2; 1.
DR Pfam; PF05833; NFACT_N; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00844};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00844}.
FT DOMAIN 421..504
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 269..296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 540 AA; 61273 MW; BDB19B000052274B CRC64;
MSFDGIFLHH MTAELQPLVG GRIQKINQPF DQELVLTVRS AGKSHKLLLS AHPVFGRVQL
TKTDFQNPQN PNNFVMILRK YLAGAFIEQI EQVGNDRQII LHISTKDEIG DSLKIALITE
IMGKHSNIIL LEKTSQKIIE SIKHIGFSQN QYRTILPGST YIAPPLNTAI DPFKATDEEI
FEALQTEQLQ QKLQGIGRDS KNALTGLSVK EFNEKLLTVT PSIYPNDTFS SIKLADEFVS
FDSLSEMLDT YYADKAERDR VKQVAASVIK KIQNELKKNR DKLKKQEREL LATDNAEIFR
QKGELLNTFL NQVPNDKASV TLENYYTNEP IEIALNPALS PVQNAQRYFH RYQKLKQAVK
FLGEQIAKTK ETIHYLESVE SNLENADVAE IADIREELIQ TGYIKQKYRN KKQKMLPPEK
YQAEDGTIIL VGKNNLQNEQ VSFKLSRRGD LWFHVKDIPG SHVLITGNAN PSDETITFAG
ELAAYFSKAR YSNLVQVDVL DVKKLHKPTG TAPGFVTYDR EKTIRVTPDE SVIKSRKIGK
//
