RQCH_STRR6
ID RQCH_STRR6 Reviewed; 551 AA.
AC Q8DQ36; Q9RNF3;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE AltName: Full=Fibronectin-binding protein PavA {ECO:0000303|PubMed:11580843};
DE AltName: Full=Pneumonococcal adherence and virulence protein A {ECO:0000303|PubMed:11580843};
GN Name=rqcH {ECO:0000255|HAMAP-Rule:MF_00844};
GN Synonyms=flpA, pavA {ECO:0000303|PubMed:11580843};
GN OrderedLocusNames=spr0868;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH HUMAN
RP FIBRONECTIN, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R800;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(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: Recombinant protein binds to immobilized human fibronectin;
CC binding is saturable and competed by heparin. Recombinant protein
CC inhibits binding of whole cells to fibronectin.
CC {ECO:0000269|PubMed:11580843}.
CC -!- SUBUNIT: Associates with stalled 50S ribosomal subunits (By
CC similarity). Interacts with human fibronectin (PubMed:11580843).
CC {ECO:0000255|HAMAP-Rule:MF_00844, ECO:0000269|PubMed:11580843}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:11580843}.
CC Cytoplasm {ECO:0000269|PubMed:11580843}. Note=Found on the cell surface
CC in the region of the capsule in capsulated bacteria (strains NCTC 10319
CC and R36A). {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}.
CC -!- CAUTION: This strain is avirulent; testing for virulence is done in
CC strain D39. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK99672.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF181976; AAF05332.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99672.1; ALT_INIT; Genomic_DNA.
DR PIR; D97980; D97980.
DR RefSeq; NP_358462.1; NC_003098.1.
DR RefSeq; WP_000006706.1; NC_003098.1.
DR PDB; 6PON; X-ray; 2.40 A; A/B=1-266.
DR PDBsum; 6PON; -.
DR AlphaFoldDB; Q8DQ36; -.
DR SMR; Q8DQ36; -.
DR STRING; 171101.spr0868; -.
DR EnsemblBacteria; AAK99672; AAK99672; spr0868.
DR GeneID; 60233470; -.
DR KEGG; spr:spr0868; -.
DR PATRIC; fig|171101.6.peg.956; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein biosynthesis; Reference proteome;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..551
FT /note="Rqc2 homolog RqcH"
FT /id="PRO_0000448047"
FT REGION 363..551
FT /note="Required for fibronectin binding"
FT /evidence="ECO:0000269|PubMed:11580843"
FT CONFLICT 102
FT /note="M -> I (in Ref. 1; AAF05332)"
FT /evidence="ECO:0000305"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:6PON"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6PON"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 97..107
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6PON"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:6PON"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6PON"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:6PON"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6PON"
FT HELIX 204..227
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:6PON"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6PON"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:6PON"
SQ SEQUENCE 551 AA; 63308 MW; 58ADEF7334CB148C 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 RHKLKKQERE
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
