ID   RBFA_DESRM              Reviewed;         120 AA.
AC   A4J5X1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=Dred_1956;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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: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; CP000612; ABO50474.1; -; Genomic_DNA.
DR   RefSeq; WP_011878284.1; NC_009253.1.
DR   AlphaFoldDB; A4J5X1; -.
DR   SMR; A4J5X1; -.
DR   STRING; 349161.Dred_1956; -.
DR   PRIDE; A4J5X1; -.
DR   EnsemblBacteria; ABO50474; ABO50474; Dred_1956.
DR   KEGG; drm:Dred_1956; -.
DR   eggNOG; COG0858; Bacteria.
DR   HOGENOM; CLU_089475_6_3_9; -.
DR   OMA; GDLQHCK; -.
DR   OrthoDB; 1971380at2; -.
DR   Proteomes; UP000001556; 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   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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..120
FT                   /note="Ribosome-binding factor A"
FT                   /id="PRO_1000070905"
SQ   SEQUENCE   120 AA;  13628 MW;  6099B6C858C26D17 CRC64;
     MSHRPERVAE AIKKEVADLI RNDIKDPRIG FVTITGVEVT RDLSFAKIFI SVMGSDAHRQ
     ETLSILQKSA GYMRSEIGRR IKLRHAPELI FKLDTSLDHG TRIAEILHEI NSQEAKPTHE