ID A0A086BP39_9BIFI Unreviewed; 219 AA.
AC A0A086BP39;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN ORFNames=BBOMB_0007 {ECO:0000313|EMBL:KFF30703.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30703.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF30703.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30703.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF30703.1}.
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DR EMBL; ATLK01000001; KFF30703.1; -; Genomic_DNA.
DR RefSeq; WP_044087735.1; NZ_JDTS01000006.1.
DR AlphaFoldDB; A0A086BP39; -.
DR STRING; 1341695.BBOMB_0007; -.
DR eggNOG; COG0858; Bacteria.
DR OrthoDB; 307788at2; -.
DR Proteomes; UP000028730; 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:UP000028730};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT REGION 149..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 219 AA; 23956 MW; A59A0EC3BEC52A07 CRC64;
MAGTNPRAAR IAALIQRVIA QTVEHQLHDK RLAGVTITDV RVTGDLQIAR VYWTQLADAG
KEQGERKRAQ QALRQATGKL RSLVGSKAGL RLTPKLQFIY DEVPSEAHEI EDILTVARKR
DEEIEKSRQN AQYAGEQDPY EHPRVRTAED FEPQYESVDG DDADYGDEWS RAQAAGSDDD
DARGVERMNG AAGASTDDAG DARPAAYDAS AQTGFSSLG
//
