ID A0A0Q4HCM9_9MICO Unreviewed; 161 AA.
AC A0A0Q4HCM9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=ASE68_12890 {ECO:0000313|EMBL:KQM83986.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM83986.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM83986.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM83986.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM83986.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM83986.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM83986.1}.
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DR EMBL; LMKQ01000001; KQM83986.1; -; Genomic_DNA.
DR RefSeq; WP_055859280.1; NZ_LMKQ01000001.1.
DR AlphaFoldDB; A0A0Q4HCM9; -.
DR STRING; 1735688.ASE68_12890; -.
DR OrthoDB; 307788at2; -.
DR Proteomes; UP000050813; 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 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00003};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT REGION 116..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 161 AA; 17760 MW; 1B56A4AA313446E3 CRC64;
MADPARARKM ADRIKEIVAR RLDKGLRDPR LGFVTITDVR VTGDLQHASI FYTVYGTDEE
RSDSALALKA ATGMLRTEVG RNITARLTPS LEFILDAIPE NADHIAALLR EARERDAETE
AAASTAEYAG DADPYVKPRD FDEDESEGDE SEDVDESATS R
//