ID   RBFA_BIFAA              Reviewed;         167 AA.
AC   A1A0A3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=BAD_0355;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of several proteins that assist in the late maturation
CC       steps of the functional core of the 30S ribosomal subunit. Associates
CC       with free 30S ribosomal subunits (but not with 30S subunits that are
CC       part of 70S ribosomes or polysomes). Required for efficient processing
CC       of 16S rRNA. May interact with the 5'-terminal helix region of 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SUBUNIT: Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal
CC       subunits or 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00003}.
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; AP009256; BAF39136.1; -; Genomic_DNA.
DR   RefSeq; WP_003808161.1; NC_008618.1.
DR   AlphaFoldDB; A1A0A3; -.
DR   SMR; A1A0A3; -.
DR   STRING; 1680.BADO_0362; -.
DR   DNASU; 4556617; -.
DR   EnsemblBacteria; BAF39136; BAF39136; BAD_0355.
DR   GeneID; 56674428; -.
DR   KEGG; bad:BAD_0355; -.
DR   HOGENOM; CLU_089475_0_1_11; -.
DR   OMA; GDLQHCK; -.
DR   Proteomes; UP000008702; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00003; RbfA; 1.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR000238; RbfA.
DR   InterPro; IPR023799; RbfA_dom_sf.
DR   InterPro; IPR020053; Ribosome-bd_factorA_CS.
DR   PANTHER; PTHR33515; PTHR33515; 1.
DR   Pfam; PF02033; RBFA; 1.
DR   SUPFAM; SSF89919; SSF89919; 1.
DR   TIGRFAMs; TIGR00082; rbfA; 1.
DR   PROSITE; PS01319; RBFA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..167
FT                   /note="Ribosome-binding factor A"
FT                   /id="PRO_0000329324"
FT   REGION          127..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..167
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   167 AA;  18785 MW;  498916BD66A8B9A5 CRC64;
     MAGTNPRAAR IAALIQRVIA SSMEAQLHDK RLANVTITEV RVTNDLQIAK VYWTQLGHEG
     HEQGERRRAQ QALNQAKGRL RSLVGTKAGL RLTPQLEFIF DEVPGEAHEI EDILALAHKR
     DEELAKSRAN AQYAGDADPY KHDEPDDDDF DDDDDVEVED WDDDDEA