YFIA_ECOL6
ID YFIA_ECOL6 Reviewed; 113 AA.
AC P0AD50; P11285;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=c3119;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 -!- 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; AE014075; AAN81568.1; -; Genomic_DNA.
DR RefSeq; WP_000178456.1; NC_004431.1.
DR AlphaFoldDB; P0AD50; -.
DR BMRB; P0AD50; -.
DR SMR; P0AD50; -.
DR STRING; 199310.c3119; -.
DR EnsemblBacteria; AAN81568; AAN81568; c3119.
DR GeneID; 67414085; -.
DR KEGG; ecc:c3119; -.
DR eggNOG; COG1544; Bacteria.
DR HOGENOM; CLU_071472_3_0_6; -.
DR OMA; DMYVAIN; -.
DR BioCyc; ECOL199310:C3119-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Acetylation; Stress response; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..113
FT /note="Ribosome-associated factor Y"
FT /id="PRO_0000169263"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 113 AA; 12785 MW; 562901F819836A87 CRC64;
MTMNITSKQM EITPAIRQHV ADRLAKLEKW QTHLINPHII LSKEPQGFVA DATINTPNGV
LVASGKHEDM YTAINELINK LERQLNKLQH KGEARRAATS VKDANFVEEV EEE