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Database: UniProt
Entry: A0A160F2M0_9BACI
LinkDB: A0A160F2M0_9BACI
Original site: A0A160F2M0_9BACI 
ID   A0A160F2M0_9BACI        Unreviewed;       118 AA.
AC   A0A160F2M0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003,
GN   ECO:0000313|EMBL:ANB60499.1};
GN   ORFNames=GFC30_1559 {ECO:0000313|EMBL:ANB60499.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB60499.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB60499.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB60499.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA   Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
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}.
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DR   EMBL; CP015438; ANB60499.1; -; Genomic_DNA.
DR   RefSeq; WP_066323924.1; NZ_CP015438.1.
DR   AlphaFoldDB; A0A160F2M0; -.
DR   KEGG; aamy:GFC30_1559; -.
DR   PATRIC; fig|294699.3.peg.1581; -.
DR   OrthoDB; 307788at2; -.
DR   Proteomes; UP000076865; Chromosome.
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:UP000076865};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
SQ   SEQUENCE   118 AA;  13552 MW;  BE6134DCC03602FB CRC64;
     MSLRATRVGE QMKKELSDII GRKLKDPRIG FVTVTDVRVT GDLQQAKVYI SVLGDEEQKK
     NTLKGLAKAT GFIRSEIGQR IRLRKTPEIY FEIDESIDYG NRIESLIREI SQEHTKEE
//
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