ID A0A2T0RBJ2_9ACTN Unreviewed; 170 AA.
AC A0A2T0RBJ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN ORFNames=CLV37_101792 {ECO:0000313|EMBL:PRY18546.1};
OS Kineococcus rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=559628 {ECO:0000313|EMBL:PRY18546.1, ECO:0000313|Proteomes:UP000238083};
RN [1] {ECO:0000313|EMBL:PRY18546.1, ECO:0000313|Proteomes:UP000238083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19711 {ECO:0000313|EMBL:PRY18546.1,
RC ECO:0000313|Proteomes:UP000238083};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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}.
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:PRY18546.1}.
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DR EMBL; PVZF01000001; PRY18546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RBJ2; -.
DR OrthoDB; 307788at2; -.
DR Proteomes; UP000238083; 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 121..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 18621 MW; 43267CB448C4F50A CRC64;
MVDPTRARKL ADRIKVVVAD ALEKRVKDPR LGFITITDAR VTNDLQHATL YYTVFGSDEE
KQGTRMALES AKGVLRSEVG RRTGIRLTPT LTFTADEVPE TAQQITELLS KAAEQDARVA
ALAAGAQPAG EPDPYKKPAD QDDAWDDEAD DEADDEADDE DEVGEDPHRA
//