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Database: UniProt
Entry: A0A1C4H420_9BIFI
LinkDB: A0A1C4H420_9BIFI
Original site: A0A1C4H420_9BIFI 
ID   A0A1C4H420_9BIFI        Unreviewed;       161 AA.
AC   A0A1C4H420;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN   ORFNames=GA0061077_0796 {ECO:0000313|EMBL:SCC79724.1};
OS   Bifidobacterium commune.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1505727 {ECO:0000313|EMBL:SCC79724.1, ECO:0000313|Proteomes:UP000242610};
RN   [1] {ECO:0000313|Proteomes:UP000242610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-52791 {ECO:0000313|Proteomes:UP000242610};
RA   Varghese N., Submissions Spin;
RL   Submitted (AUG-2016) 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:0000256|HAMAP-Rule:MF_00003}.
CC   -!- SUBUNIT: Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal
CC       subunits or 70S ribosomes. {ECO:0000256|HAMAP-Rule:MF_00003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00003}.
CC   -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00003}.
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DR   EMBL; FMBL01000002; SCC79724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4H420; -.
DR   STRING; 1505727.GA0061077_0796; -.
DR   OrthoDB; 307788at2; -.
DR   Proteomes; UP000242610; Unassembled WGS sequence.
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   NCBIfam; TIGR00082; rbfA; 1.
DR   PANTHER; PTHR33515; RIBOSOME-BINDING FACTOR A, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR33515:SF1; RIBOSOME-BINDING FACTOR A, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF02033; RBFA; 1.
DR   SUPFAM; SSF89919; Ribosome-binding factor A, RbfA; 1.
DR   PROSITE; PS01319; RBFA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242610};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT   REGION          127..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   161 AA;  18073 MW;  FADE0C14132C80B1 CRC64;
     MAGTNPRAAR IAALIQRVIA SSMERTLHDK RLKNVTITDV RVTGDLQIAR VYWTQLGDEG
     KAEGERRRAE QALKQSSGRL RTLVGAKAGL RLTPQLQFVY DEVPSEAHEI EDILTAAHRR
     DEELARTRAT AEYAGDADPY QQPREKKTAA DFEDDSVEEE Q
//
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