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Database: UniProt
Entry: U1L9R0_9MICO
LinkDB: U1L9R0_9MICO
Original site: U1L9R0_9MICO 
ID   U1L9R0_9MICO            Unreviewed;       149 AA.
AC   U1L9R0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN   ORFNames=L332_04650 {ECO:0000313|EMBL:ERG63743.1};
OS   Agrococcus pavilionensis RW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG63743.1, ECO:0000313|Proteomes:UP000016462};
RN   [1] {ECO:0000313|EMBL:ERG63743.1, ECO:0000313|Proteomes:UP000016462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW1 {ECO:0000313|EMBL:ERG63743.1,
RC   ECO:0000313|Proteomes:UP000016462};
RX   PubMed=23814108;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "First draft genome sequence from a member of the genus agrococcus,
RT   isolated from modern microbialites.";
RL   Genome Announc. 1:e00391-13(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERG63743.1}.
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DR   EMBL; ASHR01000030; ERG63743.1; -; Genomic_DNA.
DR   RefSeq; WP_021011199.1; NZ_ASHR01000030.1.
DR   AlphaFoldDB; U1L9R0; -.
DR   OrthoDB; 307788at2; -.
DR   Proteomes; UP000016462; Unassembled WGS sequence.
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:UP000016462};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT   REGION          120..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  16528 MW;  935D2435A53DF249 CRC64;
     MAENPRARKI ADRIREITVR ALEREVRDPR LGFVTITDVR VTGDLQHASI FYTVYGTDEE
     RDETAKALSS AKGVVRREIG KGLSLRLTPS IEFHLDALPE SAASIEHLLD EARQRDLAAH
     RAAEAAQYAG DADPYRKPKD ADDDETAAS
//
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