ID   RS5_MYCPN               Reviewed;         219 AA.
AC   Q50301;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=MPN_182;
GN   ORFNames=MP649;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA   Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT   "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT   pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT   ribosomal protein genes.";
RL   Nucleic Acids Res. 24:628-639(1996).
RN   [2]
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).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- FUNCTION: Located at the back of the 30S subunit body where it
CC       stabilizes the conformation of the head with respect to the body.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and
CC       S8. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and contacts
CC       protein S4. The interaction surface between S4 and S5 is involved in
CC       control of translational fidelity.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
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DR   EMBL; U34795; AAC43699.1; -; Genomic_DNA.
DR   EMBL; U00089; AAB96297.1; -; Genomic_DNA.
DR   PIR; S62804; S62804.
DR   RefSeq; NP_109870.1; NC_000912.1.
DR   RefSeq; WP_010874539.1; NC_000912.1.
DR   AlphaFoldDB; Q50301; -.
DR   SMR; Q50301; -.
DR   IntAct; Q50301; 10.
DR   STRING; 272634.MPN_182; -.
DR   EnsemblBacteria; AAB96297; AAB96297; MPN_182.
DR   GeneID; 66609170; -.
DR   KEGG; mpn:MPN_182; -.
DR   PATRIC; fig|272634.6.peg.200; -.
DR   HOGENOM; CLU_065898_2_1_14; -.
DR   OMA; KRGCGSW; -.
DR   BioCyc; MPNE272634:G1GJ3-295-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..219
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131554"
FT   DOMAIN          66..129
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  24090 MW;  50B176BEAABD80FD CRC64;
     MTDQNQKANQ GNGLQTTNLQ AHAQRKHNLR PSSEGIKKAV SKKEGGGHNR NNQNRRFQKP
     AFKSEFEERI VKLKRISKTT KGGRNMRFSV LVVVGNRKGK IGYGIAKALE VPNAIKKAIK
     AAHNSLHTIE IHKGSIYHEV IGRSGASRVL LKPAPQGTGI IAGGAIRAII ELAGYSDIYT
     KNLGRNTPIN MIHATMDGIL KQLSPRRVAI LRNKNLNEL