ID   RQCH_STRP2              Reviewed;         551 AA.
AC   A0A0H2ZPC8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Rqc2 homolog RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE            Short=RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE   AltName: Full=Pneumonococcal adherence and virulence protein A {ECO:0000303|PubMed:11580843};
GN   Name=rqcH {ECO:0000255|HAMAP-Rule:MF_00844};
GN   Synonyms=pavA {ECO:0000303|PubMed:11580843}; OrderedLocusNames=SPD_0854;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=D39 / NCTC 7466, NCTC 10319, and R36A;
RX   PubMed=11580843; DOI=10.1046/j.1365-2958.2001.02610.x;
RA   Holmes A.R., McNab R., Millsap K.W., Rohde M., Hammerschmidt S.,
RA   Mawdsley J.L., Jenkinson H.F.;
RT   "The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding
RT   protein that is essential for virulence.";
RL   Mol. Microbiol. 41:1395-1408(2001).
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:0000255|HAMAP-Rule:MF_00844}.
CC   -!- FUNCTION: Plays a significant role in virulence (PubMed:11580843).
CC       Recombinant protein binds to immobilized human fibronectin; binding is
CC       saturable and competed by heparin. Purified protein inhibits binding of
CC       whole cells to fibronectin (By similarity).
CC       {ECO:0000250|UniProtKB:Q8DQ36, ECO:0000269|PubMed:11580843}.
CC   -!- SUBUNIT: Associates with stalled 50S ribosomal subunits (By
CC       similarity). Interacts with human fibronectin (By similarity).
CC       {ECO:0000250|UniProtKB:Q8DQ36, ECO:0000255|HAMAP-Rule:MF_00844}.
CC   -!- SUBCELLULAR LOCATION: Secreted, capsule {ECO:0000269|PubMed:11580843}.
CC       Cell surface {ECO:0000250|UniProtKB:Q8DQ36}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8DQ36}. Note=Found on the cell surface in the
CC       region of the capsule in capsulated bacteria (NCTC 10319 and R36A).
CC       {ECO:0000269|PubMed:11580843}.
CC   -!- DISRUPTION PHENOTYPE: About 50% reduction of binding to immobilized
CC       human fibronectin, greatly reduced mortality in mice (tested with
CC       encapsulated strain D39). {ECO:0000269|PubMed:11580843}.
CC   -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00844}.
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DR   EMBL; CP000410; ABJ54581.1; -; Genomic_DNA.
DR   RefSeq; WP_000006705.1; NC_008533.2.
DR   AlphaFoldDB; A0A0H2ZPC8; -.
DR   SMR; A0A0H2ZPC8; -.
DR   STRING; 373153.SPD_0854; -.
DR   EnsemblBacteria; ABJ54581; ABJ54581; SPD_0854.
DR   KEGG; spd:SPD_0854; -.
DR   eggNOG; COG1293; Bacteria.
DR   HOGENOM; CLU_022481_2_1_9; -.
DR   OMA; SKPGFVI; -.
DR   OrthoDB; 713667at2; -.
DR   Proteomes; UP000001452; Chromosome.
DR   GO; GO:0042603; C:capsule; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   HAMAP; MF_00844_B; RqcH_B; 1.
DR   InterPro; IPR008532; NFACT_RNA-bd.
DR   InterPro; IPR043682; RqcH_bacterial.
DR   Pfam; PF05670; NFACT-R_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis; RNA-binding; Secreted; tRNA-binding;
KW   Virulence.
FT   CHAIN           1..551
FT                   /note="Rqc2 homolog RqcH"
FT                   /id="PRO_0000448046"
SQ   SEQUENCE   551 AA;  63280 MW;  50A0EF7332F6148C CRC64;
     MSFDGFFLHH IVEELRSELV NGRIQKINQP FEQELVLQIR SNRQSHRLLL SAHPVFGRIQ
     LTQTTFENPA QPSTFIMVLR KYLQGALIES IEQVENDRIV EMTVSNKNEI GDHIQATLII
     EIMGKHSNIL LVDKSSHKIL EVIKHVGFSQ NSYRTLLPGS TYIAPPSTES LNPFTIKDEK
     LFEILQTQEL TAKNLQSLFQ GLGRDTANEL ERILVSEKLS AFRNFFNQET KPCLTETSFS
     PVPFANQAGE PFANLSDLLD TYYKNKAERD RVKQQASELI RRVENELQKN RHKLKKQEKE
     LLATDNAEEF RQKGELLTTF LHQVPNDQDQ VILDNYYTNQ PIMIALDKAL TPNQNAQRYF
     KRYQKLKEAV KYLTDLIEET KATILYLESV ETVLNQAGLE EIAEIREELI QTGFIRRRQR
     EKIQKRKKLE QYLASDGKTI IYVGRNNLQN EELTFKMARK EELWFHAKDI PGSHVVISGN
     LDPSDAVKTD AAELAAYFSQ GRLSNLVQVD MIEVKKLNKP TGGKPGFVTY TGQKTLRVTP
     DSKKIASMKK S