ID   RQCH_BACNB              Reviewed;         570 AA.
AC   D4FWG0;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
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 YloA {ECO:0000303|PubMed:28294433};
GN   Name=rqcH {ECO:0000255|HAMAP-Rule:MF_00844};
GN   Synonyms=yloA {ECO:0000303|PubMed:28294433}; ORFNames=BSNT_08076;
OS   Bacillus subtilis subsp. natto (strain BEST195).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=645657;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEST195;
RX   PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA   Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA   Itaya M., Sakakibara Y.;
RT   "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT   from very short read data.";
RL   BMC Genomics 11:243-243(2010).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=BEST195;
RX   PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA   Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT   "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT   long reads with high-quality short reads.";
RL   PLoS ONE 9:E109999-E109999(2014).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=RG4365;
RX   PubMed=28294433; DOI=10.1111/mmi.13666;
RA   Rodriguez Ayala F., Bauman C., Bartolini M., Saball E., Salvarrey M.,
RA   Lenini C., Cogliati S., Strauch M., Grau R.;
RT   "Transcriptional regulation of adhesive properties of Bacillus subtilis to
RT   extracellular matrix proteins through the fibronectin-binding protein
RT   YloA.";
RL   Mol. Microbiol. 104:804-821(2017).
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 role in bacterial binding to eukaryotic host
CC       fibronectin and other extracellular matrix proteins (Probable). Wild-
CC       type cells inhibit binding of S.aureus, L.monocytogenes and E.faecalis
CC       to human fibronectin in vitro, bacteria with a deletion of this gene no
CC       longer do so (PubMed:28294433). {ECO:0000269|PubMed:28294433,
CC       ECO:0000305|PubMed:28294433}.
CC   -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00844}.
CC   -!- INDUCTION: Expressed during exponential growth, decreases in stationary
CC       phase. Transcription is down-regulated by AbrB and DegU in logarithmic
CC       and stationary phase respectively. {ECO:0000269|PubMed:28294433}.
CC   -!- DISRUPTION PHENOTYPE: Bacteria no longer adhere to fibronectin or
CC       collagen, decreased biofilm formation. Bacteria no longer inhibit
CC       binding of other bacteria to fibronectin.
CC       {ECO:0000269|PubMed:28294433}.
CC   -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00844}.
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DR   EMBL; AP011541; BAI85191.1; -; Genomic_DNA.
DR   RefSeq; WP_014479755.1; NC_017196.2.
DR   AlphaFoldDB; D4FWG0; -.
DR   SMR; D4FWG0; -.
DR   STRING; 86029.AWV81_08705; -.
DR   EnsemblBacteria; BAI85191; BAI85191; BSNT_08076.
DR   KEGG; bso:BSNT_08076; -.
DR   PATRIC; fig|645657.3.peg.2607; -.
DR   HOGENOM; CLU_022481_2_1_9; -.
DR   Proteomes; UP000006805; 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   2: Evidence at transcript level;
KW   Cell adhesion; Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN           1..570
FT                   /note="Rqc2 homolog RqcH"
FT                   /id="PRO_0000448045"
SQ   SEQUENCE   570 AA;  65108 MW;  3F32B086C6CCB2F6 CRC64;
     MSFDGMFTYG MTHELNEKIM GGRITKVHQP YKHDVIFHIR AKGKNQKLLL SAHPSYSRVH
     ITAQAYENPS EPPMFCMLLR KHIEGGFIEK IEQAGLDRIM IFHIKSRNEI GDETVRKLYV
     EIMGRHSNII LTDAAENVII DGLKHLSPSM NSYRTVLPGQ DYKLPPAQDK ISPLEASEDD
     ILRHLSFQEG KLDKQIVDHF SGVSPLFAKE AVHRAGLANK VTLPKALLAL FAEVKEHRFI
     PNITTVNGKE YFYLLELTHL KGEARSFESL 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