RBFA_MYCPN
ID RBFA_MYCPN Reviewed; 116 AA.
AC P75589;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003, ECO:0000303|PubMed:15185964};
GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=MPN_156;
GN ORFNames=MP675;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=15185964; DOI=10.1023/b:jsfg.0000016127.57320.82;
RA Rubin S.M., Pelton J.G., Yokota H., Kim R., Wemmer D.E.;
RT "Solution structure of a putative ribosome binding protein from Mycoplasma
RT pneumoniae and comparison to a distant homolog.";
RL J. Struct. Funct. Genomics 4:235-243(2003).
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 (PubMed:15185964). Binds 30S ribosomal subunits, but
CC not 50S ribosomal subunits or 70S ribosomes. {ECO:0000255|HAMAP-
CC Rule:MF_00003, ECO:0000305|PubMed:15185964}.
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; U00089; AAB96323.1; -; Genomic_DNA.
DR PIR; S74001; S74001.
DR RefSeq; NP_109844.1; NC_000912.1.
DR RefSeq; WP_010874513.1; NC_000912.1.
DR PDB; 1PA4; NMR; -; A=1-116.
DR PDBsum; 1PA4; -.
DR AlphaFoldDB; P75589; -.
DR BMRB; P75589; -.
DR SMR; P75589; -.
DR IntAct; P75589; 2.
DR STRING; 272634.MPN_156; -.
DR PRIDE; P75589; -.
DR EnsemblBacteria; AAB96323; AAB96323; MPN_156.
DR GeneID; 66609196; -.
DR KEGG; mpn:MPN_156; -.
DR PATRIC; fig|272634.6.peg.174; -.
DR HOGENOM; CLU_089475_6_5_14; -.
DR OMA; IYIDCLI; -.
DR BioCyc; MPNE272634:G1GJ3-263-MON; -.
DR EvolutionaryTrace; P75589; -.
DR Proteomes; UP000000808; 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 Pfam; PF02033; RBFA; 1.
DR SUPFAM; SSF89919; SSF89919; 1.
DR TIGRFAMs; TIGR00082; rbfA; 1.
DR PROSITE; PS01319; RBFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..116
FT /note="Ribosome-binding factor A"
FT /id="PRO_0000102695"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:1PA4"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1PA4"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1PA4"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1PA4"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1PA4"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1PA4"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1PA4"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:1PA4"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:1PA4"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1PA4"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1PA4"
SQ SEQUENCE 116 AA; 13389 MW; EBF11E251DE30720 CRC64;
MASYKKERLE NDIIRLINRT VIHEIYNETV KTGHVTHVKL SDDLLHVTVY LDCYNREQID
RVVGAFNQAK GVFSRVLAHN LYLAKAVQIH FVKDKAIDNA MRIESIINSL KKSKPN