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Database: UniProt
Entry: A0A2T0RBJ2_9ACTN
LinkDB: A0A2T0RBJ2_9ACTN
Original site: A0A2T0RBJ2_9ACTN 
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
//
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