RQCH_STRSY
ID RQCH_STRSY Reviewed; 552 AA.
AC A4VWG9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000255|HAMAP-Rule:MF_00844};
DE AltName: Full=Anchorless FBPS {ECO:0000303|PubMed:27834729};
DE AltName: Full=Fibronectin-binding protein {ECO:0000303|PubMed:27834729};
GN Name=rqcH {ECO:0000255|HAMAP-Rule:MF_00844};
GN Synonyms=fbpS {ECO:0000303|PubMed:27834729}; OrderedLocusNames=SSU05_1492;
OS Streptococcus suis (strain 05ZYH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05ZYH33;
RX PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA Yang R., Wang J., Yu J.;
RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT of S. suis 2 Chinese isolates.";
RL PLoS ONE 2:E315-E315(2007).
RN [2] {ECO:0007744|PDB:5H3W, ECO:0007744|PDB:5H3X}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-268, X-RAY CRYSTALLOGRAPHY
RP (2.60 ANGSTROMS) OF 271-552, INTERACTION WITH HOST FIBRONECTIN (FN1),
RP DOMAIN, DISRUPTION PHENOTYPE, AND COILED COIL.
RC STRAIN=05ZYH33;
RX PubMed=27834729; DOI=10.1073/pnas.1608406113;
RA Musyoki A.M., Shi Z., Xuan C., Lu G., Qi J., Gao F., Zheng B., Zhang Q.,
RA Li Y., Haywood J., Liu C., Yan J., Shi Y., Gao G.F.;
RT "Structural and functional analysis of an anchorless fibronectin-binding
RT protein FBPS from Gram-positive bacterium Streptococcus suis.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13869-13874(2016).
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 -!- SUBUNIT: Associates with stalled 50S ribosomal subunits (By
CC similarity). Recombinant protein interacts with the N-terminal 30 kDa
CC of human fibronectin (FN1) (PubMed:27834729). {ECO:0000255|HAMAP-
CC Rule:MF_00844, ECO:0000269|PubMed:27834729}.
CC -!- DOMAIN: The N-terminus (residues 1-268) and C-terminus (271-552) form 2
CC separate domains; the N-terminus is globular while the C-terminus is
CC elongated. The N-terminus binds to S.suis cells while the C-terminus
CC binds to human HEp-2 cells. Incubation with the C-terminus stimulates
CC ERK and p38 phosphorylation in HEp-2 cells.
CC {ECO:0000269|PubMed:27834729}.
CC -!- DISRUPTION PHENOTYPE: About 25% decreased adherence to human HEp-2
CC cells, about 50% decrease in binding to immobilized fibronectin. HEp-2
CC cells treated with mutant bacteria secrete less IL-6 and IL-8, activate
CC ERK and p38 more slowly and to a lesser extent than with wild-type
CC bacteria. {ECO:0000269|PubMed:27834729}.
CC -!- MISCELLANEOUS: Repeated attempts to crystallize a full-length protein
CC yields proteins cleaved between the N- and C-terminal domains.
CC {ECO:0000269|PubMed:27834729}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000255|HAMAP-
CC Rule:MF_00844}.
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DR EMBL; CP000407; ABP90458.1; -; Genomic_DNA.
DR PDB; 5H3W; X-ray; 2.60 A; A=272-552, B=271-552.
DR PDB; 5H3X; X-ray; 2.10 A; A=2-268.
DR PDBsum; 5H3W; -.
DR PDBsum; 5H3X; -.
DR AlphaFoldDB; A4VWG9; -.
DR SMR; A4VWG9; -.
DR STRING; 391295.SSU05_1492; -.
DR EnsemblBacteria; ABP90458; ABP90458; SSU05_1492.
DR KEGG; ssu:SSU05_1492; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR OMA; SKPGFVI; -.
DR BioCyc; SSUI391295:GHI8-1545-MON; -.
DR Proteomes; UP000000243; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Coiled coil; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..552
FT /note="Rqc2 homolog RqcH"
FT /id="PRO_0000448048"
FT COILED 271..317
FT /evidence="ECO:0000269|PubMed:27834729"
FT COILED 357..398
FT /evidence="ECO:0000269|PubMed:27834729"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:5H3X"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 97..107
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5H3X"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:5H3X"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:5H3X"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:5H3X"
FT HELIX 274..304
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 358..397
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 401..413
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 487..499
FT /evidence="ECO:0007829|PDB:5H3W"
FT TURN 502..505
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 506..515
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5H3W"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:5H3W"
FT HELIX 544..549
FT /evidence="ECO:0007829|PDB:5H3W"
SQ SEQUENCE 552 AA; 63301 MW; 830AC44397B67467 CRC64;
MSFDGFFLHH MTAELRANLE GGRIQKINQP FEQEIVLNIR SNRQSHKLLL SAHSVFGRVQ
LTQSDFTNPK VPNTFTMILR KYLQGAIIEE IRQLDNDRIL EFSVSNKDEI GDHIQATLIV
EIMGKHSNII LVDKSEQKII EAIKHVGFSQ NSYRTILPGS TYIRPPETHS LNPYTVSDEK
LFEILSTQEL SPKNLQQVFQ GLGRDTASEL ANHLQIDRLK NFRAFFDQAT QPSLTDKSYA
ALPFANSPEN QPHFESLSSL LDFYYQDKAE RDRVAQQANE LIKRVASELE KNRKKLIKQE
QELADTETAE LVRQKGELLT TYLHQVPNDQ SSVRLDNYYT GKELEIELDV ALTPSQNAQR
YFKKYQKLKE AVKHLTNLIE ETKSTIVYLE SVDTMLGQAS LAEIDEIREE LIETGYLKRR
HREKIHKRQK PERYLATDGK TIILVGKNNL QNDELTFKMA KKGELWFHAK DIPGSHVVIT
DNLDPSDEVK TDAAELAAYF SKARHSNLVQ VDMIEAKKLH KPTGGKPGFV TYRGQKTLRV
TPTEDKIKSM KI
