RBFA_STAA8
ID RBFA_STAA8 Reviewed; 116 AA.
AC Q2G2Q4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003};
GN OrderedLocusNames=SAOUHSC_01247;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (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:0000255|HAMAP-Rule:MF_00003}.
CC -!- SUBUNIT: Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal
CC subunits or 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003}.
CC -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP-
CC Rule:MF_00003}.
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DR EMBL; CP000253; ABD30348.1; -; Genomic_DNA.
DR RefSeq; WP_000097322.1; NZ_LS483365.1.
DR RefSeq; YP_499780.1; NC_007795.1.
DR PDB; 6YE5; NMR; -; A=2-116.
DR PDBsum; 6YE5; -.
DR AlphaFoldDB; Q2G2Q4; -.
DR SMR; Q2G2Q4; -.
DR STRING; 1280.SAXN108_1274; -.
DR EnsemblBacteria; ABD30348; ABD30348; SAOUHSC_01247.
DR GeneID; 3919978; -.
DR KEGG; sao:SAOUHSC_01247; -.
DR PATRIC; fig|93061.5.peg.1141; -.
DR eggNOG; COG0858; Bacteria.
DR HOGENOM; CLU_089475_6_3_9; -.
DR OMA; GDLQHCK; -.
DR PRO; PR:Q2G2Q4; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
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 PANTHER; PTHR33515; PTHR33515; 1.
DR Pfam; PF02033; RBFA; 1.
DR SUPFAM; SSF89919; SSF89919; 1.
DR TIGRFAMs; TIGR00082; rbfA; 1.
DR PROSITE; PS01319; RBFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..116
FT /note="Ribosome-binding factor A"
FT /id="PRO_1000000221"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:6YE5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6YE5"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6YE5"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:6YE5"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:6YE5"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:6YE5"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6YE5"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6YE5"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6YE5"
SQ SEQUENCE 116 AA; 13515 MW; 9438DBA0E3B69289 CRC64;
MSSMRAERVG EQMKKELMDI INNKVKDPRV GFITITDVVL TNDLSQAKVF LTVLGNDKEV
ENTFKALDKA KGFIKSELGS RMRLRIMPEL MYEYDQSIEY GNKIERMIQD LHKQDR
