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Database: UniProt
Entry: A0A1B1N7L5_9MICO
LinkDB: A0A1B1N7L5_9MICO
Original site: A0A1B1N7L5_9MICO 
ID   A0A1B1N7L5_9MICO        Unreviewed;       156 AA.
AC   A0A1B1N7L5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000256|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000256|HAMAP-Rule:MF_00003};
GN   ORFNames=SGUI_0021 {ECO:0000313|EMBL:ANS77417.1};
OS   Serinicoccus hydrothermalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Serinicoccus.
OX   NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS77417.1, ECO:0000313|Proteomes:UP000092482};
RN   [1] {ECO:0000313|EMBL:ANS77417.1, ECO:0000313|Proteomes:UP000092482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT9 {ECO:0000313|EMBL:ANS77417.1,
RC   ECO:0000313|Proteomes:UP000092482};
RA   Tang K.;
RT   "Shallow-sea hydrothermal system.";
RL   Submitted (MAR-2016) 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: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}.
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DR   EMBL; CP014989; ANS77417.1; -; Genomic_DNA.
DR   RefSeq; WP_066634696.1; NZ_CP014989.1.
DR   AlphaFoldDB; A0A1B1N7L5; -.
DR   STRING; 1758689.SGUI_0021; -.
DR   KEGG; serj:SGUI_0021; -.
DR   PATRIC; fig|1758689.4.peg.22; -.
DR   OrthoDB; 307788at2; -.
DR   Proteomes; UP000092482; 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   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:UP000092482};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00003}.
FT   REGION          119..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  17159 MW;  7C94232154A62143 CRC64;
     MVDQARARRI AERTKQLVTQ GLSQVVKDER VGFVTITDVR VTGDLQHASV FYTVLGSDTD
     RETAAEILEA YRGRLRSFVG KGLGIRLTPT LEFILDALPE DAQHMDDLLR RVAARDAELA
     AGRSSSGYAG EADPYRKPRT DETEAEDDAP GVADPR
//
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