RQCH_BACSU
ID RQCH_BACSU Reviewed; 570 AA.
AC O34693; Q796I2; Q799L3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000255|HAMAP-Rule:MF_00844, ECO:0000303|PubMed:31155236};
DE Short=RqcH {ECO:0000255|HAMAP-Rule:MF_00844, ECO:0000303|PubMed:31155236};
GN Name=rqcH {ECO:0000255|HAMAP-Rule:MF_00844, ECO:0000303|PubMed:31155236};
GN Synonyms=yloA; OrderedLocusNames=BSU15640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of
RT the pyr operon.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-198.
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [4]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17586671; DOI=10.1128/aem.00472-07;
RA Lulko A.T., Veening J.-W., Buist G., Smits W.K., Blom E.J., Beekman A.C.,
RA Bron S., Kuipers O.P.;
RT "Production and secretion stress caused by overexpression of heterologous
RT alpha-amylase leads to inhibition of sporulation and a prolonged motile
RT phase in Bacillus subtilis.";
RL Appl. Environ. Microbiol. 73:5354-5362(2007).
RN [5]
RP SEQUENCE REVISION TO START SITE, FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 97-ASP-ARG-98; ASP-97 AND 121-GLU--MET-123.
RC STRAIN=168 / 1A700;
RX PubMed=31155236; DOI=10.1016/j.cell.2019.05.002;
RA Lytvynenko I., Paternoga H., Thrun A., Balke A., Mueller T.A., Chiang C.H.,
RA Nagler K., Tsaprailis G., Anders S., Bischofs I., Maupin-Furlow J.A.,
RA Spahn C.M.T., Joazeiro C.A.P.;
RT "Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality
RT Control.";
RL Cell 0:0-0(2019).
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 Selectively binds tRNA(Ala)(UGC), which is presumably the sole source
CC of tRNA(Ala) used for Ala tailing directed by this protein. May add
CC between 1 and at least 8 Ala residues; detection of the Ala tail
CC requires either deletion of clpP or its inhibition. Binds to 50S
CC ribosomal subunits, at least 30% of which contain a P-site tRNA and
CC thus are obstructed. {ECO:0000269|PubMed:31155236}.
CC -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00844, ECO:0000269|PubMed:31155236}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during stationary phase.
CC {ECO:0000269|PubMed:17586671}.
CC -!- INDUCTION: Up-regulated under secretion stress conditions, possibly in
CC a CssR/CssS-dependent manner. {ECO:0000269|PubMed:17586671}.
CC -!- DISRUPTION PHENOTYPE: Not essential in rich media; synthetic growth
CC defects are seen in double rqcH ssrA mutants, further exacerbated by
CC translational inhibitors spectinomycin and erythromycin or at elevated
CC temperatures. Decreased accumulation of a stalled reporter protein.
CC Triple rqcH clpP ssrA mutants cannot be generated.
CC {ECO:0000269|PubMed:31155236}.
CC -!- MISCELLANEOUS: Activity of this protein is best tested in a clpP or
CC ssrA deletion mutant; ssrA (tmRNA) encodes the SsrA tag added to
CC nascent proteins in stalled ribosomes by trans-translation, which
CC targets the nascent protein for degradation.
CC {ECO:0000269|PubMed:31155236}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000255|HAMAP-
CC Rule:MF_00844}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA04416.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:31155236};
CC Sequence=CAA74268.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:31155236};
CC Sequence=CAB13438.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:31155236};
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DR EMBL; AJ000974; CAA04416.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13438.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y13937; CAA74268.1; ALT_INIT; Genomic_DNA.
DR PIR; G69877; G69877.
DR RefSeq; NP_389447.1; NC_000964.3.
DR RefSeq; WP_003232089.1; NZ_JNCM01000035.1.
DR RefSeq; WP_010886504.1; NC_000964.3.
DR PDB; 7AQC; EM; 2.99 A; R=1-570.
DR PDB; 7AQD; EM; 3.10 A; R=1-570.
DR PDB; 7AS8; EM; 2.90 A; 0=1-570.
DR PDB; 7AS9; EM; 3.50 A; 0=1-570.
DR PDB; 7ASA; EM; 3.50 A; 0=1-570.
DR PDB; 7OPE; EM; 3.20 A; 0=1-570.
DR PDBsum; 7AQC; -.
DR PDBsum; 7AQD; -.
DR PDBsum; 7AS8; -.
DR PDBsum; 7AS9; -.
DR PDBsum; 7ASA; -.
DR PDBsum; 7OPE; -.
DR AlphaFoldDB; O34693; -.
DR SMR; O34693; -.
DR STRING; 224308.BSU15640; -.
DR PaxDb; O34693; -.
DR PRIDE; O34693; -.
DR EnsemblBacteria; CAB13438; CAB13438; BSU_15640.
DR GeneID; 936878; -.
DR KEGG; bsu:BSU15640; -.
DR PATRIC; fig|224308.43.peg.1659; -.
DR eggNOG; COG1293; Bacteria.
DR InParanoid; O34693; -.
DR PhylomeDB; O34693; -.
DR BioCyc; BSUB:BSU15640-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
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; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..570
FT /note="Rqc2 homolog RqcH"
FT /id="PRO_0000383595"
FT MUTAGEN 97..98
FT /note="DR->YA: No longer binds tRNA(Ala) anticodon (UGC),
FT loss of Ala tailing ability, decreased accumulation of a
FT stalled reporter protein."
FT /evidence="ECO:0000269|PubMed:31155236"
FT MUTAGEN 97
FT /note="D->Y: No longer binds tRNA(Ala) anticodon (UGC), has
FT minor Ala tailing ability, decreased accumulation of a
FT stalled reporter protein."
FT /evidence="ECO:0000269|PubMed:31155236"
FT MUTAGEN 121..123
FT /note="EIM->AAA: No longer binds tRNA(Ala) anticodon (UGC),
FT decreased accumulation of a stalled reporter protein."
FT /evidence="ECO:0000269|PubMed:31155236"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 97..107
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7AS9"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7ASA"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 270..316
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7ASA"
FT HELIX 369..412
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 467..476
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 480..492
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:7AQC"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 570 AA; 65205 MW; 4E6C9EF2F62828C8 CRC64;
MSFDGMFTYG MTHELNEKIM GGRITKIHQP YKHDVIFHIR AKGKNQKLLL SAHPSYSRVH
ITAQAYENPS EPPMFCMLLR KHIEGGFIEK IEQAGLDRIM IFHIKSRNEI GDETVRKLYV
EIMGRHSNII LTDAAENVII DGLKHLSPSM NSYRTVLPGQ DYKLPPAQDK ISPLEASEDD
ILRHLSFQEG RLDKQIVDHF SGVSPLFAKE AVHRAGLANK VTLPKALLAL FAEVKEHRFI
PNITTVNGKE YFYLLELTHL KGEARRFDSL SELLDRFYFG KAERDRVKQQ AQDLERFVVN
ERKKNANKIK KLEKTLEYSE NAKEFQLYGE LLTANLYMLK KGDKQAEVIN YYDEESPTIT
IPLNPNKTPS ENAQAYFTKY QKAKNSVAVV EEQIRLAQEE IEYFDQLIQQ LSSASPRDIS
EIREELVEGK YLRPKQQKGQ KKQKPHNPVL ETYESTSGLT ILVGKNNRQN EYLTTRVAAR
DDIWLHTKDI PGSHVVIRSS EPDEQTIMEA ATIAAYFSKA KDSSSVPVDY TKIRHVKKPN
GAKPGFVTYD SQHTVFVTPD ADTVIKLKKS
