ID   RBFA_CLAMS              Reviewed;         170 AA.
AC   B0RDY8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=CMS1842;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ01947.1; -; Genomic_DNA.
DR   RefSeq; WP_012299186.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0RDY8; -.
DR   SMR; B0RDY8; -.
DR   STRING; 31964.CMS1842; -.
DR   PRIDE; B0RDY8; -.
DR   EnsemblBacteria; CAQ01947; CAQ01947; CMS1842.
DR   KEGG; cms:CMS1842; -.
DR   eggNOG; COG0858; Bacteria.
DR   HOGENOM; CLU_089475_0_0_11; -.
DR   OMA; GDLQHCK; -.
DR   Proteomes; UP000001318; 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   PANTHER; PTHR33515; PTHR33515; 1.
DR   Pfam; PF02033; RBFA; 1.
DR   SUPFAM; SSF89919; SSF89919; 1.
DR   TIGRFAMs; TIGR00082; rbfA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..170
FT                   /note="Ribosome-binding factor A"
FT                   /id="PRO_1000073754"
FT   REGION          123..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   170 AA;  18586 MW;  6FEEAB31FD271609 CRC64;
     MVDHARARKM ADRIKEIVAR KLDRGIKDPR LGFVTVTDVR VTGDLQHASI FYTVYGTDEE
     RADTAAALKS ATGMLRSEVG KNITARLTPS LEFILDGVPE NAAAIDALLE EARRRDADVQ
     AQAKAGVYAG DEDPYVKPRV IGEDEDDDDE EGDEDGDDVD RSAPGYEPAH