ID A0A261ESF9_9BIFI Unreviewed; 210 AA.
AC A0A261ESF9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN ORFNames=PSRA_1602 {ECO:0000313|EMBL:OZG49797.1};
OS Pseudoscardovia radai.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Pseudoscardovia.
OX NCBI_TaxID=987066 {ECO:0000313|EMBL:OZG49797.1, ECO:0000313|Proteomes:UP000216725};
RN [1] {ECO:0000313|EMBL:OZG49797.1, ECO:0000313|Proteomes:UP000216725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24742 {ECO:0000313|EMBL:OZG49797.1,
RC ECO:0000313|Proteomes:UP000216725};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG49797.1}.
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DR EMBL; MWWR01000018; OZG49797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261ESF9; -.
DR OrthoDB; 307788at2; -.
DR Proteomes; UP000216725; 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 Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT REGION 129..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23111 MW; D92E38703A1E1FF9 CRC64;
MAGTNPRAVR VAGLIQRVVA TALQRDLRDP RLAHVTITEV RVTNDLQIAR IYWTYLGDDG
HERGQRKRAK QALQQSAGRL RSMVGRKAGL RLTPQLQFIY DEVPAEATEV EDVLTVALKR
DQELAKLREN ATYAGDADPY RHDDERKGAD SADSDDSEGV DGAYGAGYGD YDDDGEYDDS
DVDFPDDDED IDDDDDTADD ASAGDGDSAR
//
