ID   RBFA_LEPBP              Reviewed;         149 AA.
AC   B0SQH5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=LEPBI_I1526;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(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; CP000786; ABZ97633.1; -; Genomic_DNA.
DR   RefSeq; WP_012388512.1; NC_010602.1.
DR   AlphaFoldDB; B0SQH5; -.
DR   SMR; B0SQH5; -.
DR   STRING; 456481.LEPBI_I1526; -.
DR   KEGG; lbi:LEPBI_I1526; -.
DR   HOGENOM; CLU_089475_5_0_12; -.
DR   OMA; CSLSINH; -.
DR   OrthoDB; 1971380at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS07510-MON; -.
DR   Proteomes; UP000001847; Chromosome I.
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..149
FT                   /note="Ribosome-binding factor A"
FT                   /id="PRO_1000088902"
FT   REGION          116..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..139
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  17078 MW;  E9D602EF492CE480 CRC64;
     MNPIRMKKLE SEIIRQISTA ILEGKVKDPR VFLPSFHRIE ISEDLKYAKV YFTALCNNNE
     RKKLTQGLVS CAGFLSSFVG KNLRLHTNPK FTFVWDNSYI KSLEVNRLID DSAPKTLFEE
     LHPNPEEDDG DTDAETLLED SESGIERET