ID   YFIA_HAEIN              Reviewed;         107 AA.
AC   P71346;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Ribosome-associated factor Y {ECO:0000305};
DE            Short=pY;
DE   AltName: Full=Ribosome associated inhibitor A;
GN   Name=yfiA {ECO:0000305}; Synonyms=raiA; OrderedLocusNames=HI_0257;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   STRUCTURE BY NMR, AND MASS SPECTROMETRY.
RX   PubMed=11551193; DOI=10.1021/bi011077i;
RA   Parsons L., Eisenstein E., Orban J.;
RT   "Solution structure of HI0257, a bacterial ribosome binding protein.";
RL   Biochemistry 40:10979-10986(2001).
CC   -!- FUNCTION: During stationary phase, prevents 70S dimer formation,
CC       probably in order to regulate translation efficiency during transition
CC       between the exponential and the stationary phases. In addition, during
CC       environmental stress such as cold shock or excessive cell density at
CC       stationary phase, stabilizes the 70S ribosome against dissociation,
CC       inhibits translation initiation and increase translation accuracy. When
CC       normal growth conditions are restored, is quickly released from the
CC       ribosome (By similarity). {ECO:0000250|UniProtKB:P0AD49}.
CC   -!- SUBUNIT: Associates mainly with 70S ribosomes.
CC       {ECO:0000250|UniProtKB:P0AD49}.
CC   -!- INDUCTION: By environmental stress and during stationary phase.
CC       {ECO:0000250|UniProtKB:P0AD49}.
CC   -!- MASS SPECTROMETRY: Mass=12473.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11551193};
CC   -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC       YfiA subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC21923.1; -; Genomic_DNA.
DR   RefSeq; NP_438426.1; NC_000907.1.
DR   RefSeq; WP_005653397.1; NC_000907.1.
DR   PDB; 1IMU; NMR; -; A=1-107.
DR   PDBsum; 1IMU; -.
DR   AlphaFoldDB; P71346; -.
DR   BMRB; P71346; -.
DR   SMR; P71346; -.
DR   STRING; 71421.HI_0257; -.
DR   EnsemblBacteria; AAC21923; AAC21923; HI_0257.
DR   KEGG; hin:HI_0257; -.
DR   PATRIC; fig|71421.8.peg.272; -.
DR   eggNOG; COG1544; Bacteria.
DR   HOGENOM; CLU_071472_3_0_6; -.
DR   OMA; DMYVAIN; -.
DR   PhylomeDB; P71346; -.
DR   BioCyc; HINF71421:G1GJ1-271-MON; -.
DR   EvolutionaryTrace; P71346; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0045900; P:negative regulation of translational elongation; IBA:GO_Central.
DR   GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
DR   CDD; cd00552; RaiA; 1.
DR   Gene3D; 3.30.160.100; -; 1.
DR   InterPro; IPR036567; RHF-like.
DR   InterPro; IPR003489; RHF/RaiA.
DR   Pfam; PF02482; Ribosomal_S30AE; 1.
DR   SUPFAM; SSF69754; SSF69754; 1.
DR   TIGRFAMs; TIGR00741; yfiA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Stress response; Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..107
FT                   /note="Ribosome-associated factor Y"
FT                   /id="PRO_0000169265"
FT   REGION          85..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:1IMU"
FT   HELIX           14..28
FT                   /evidence="ECO:0007829|PDB:1IMU"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:1IMU"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:1IMU"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:1IMU"
FT   HELIX           70..90
FT                   /evidence="ECO:0007829|PDB:1IMU"
SQ   SEQUENCE   107 AA;  12191 MW;  60708BA29CA334E2 CRC64;
     MTLNITSKQM DITPAIREHL EERLAKLGKW QTQLISPHFV LNKVPNGFSV EASIGTPLGN
     LLASATSDDM YKAINEVEEK LERQLNKLQH KSESRRADER LKDSFEN