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RS5_MYCLE
ID   RS5_MYCLE               Reviewed;         217 AA.
AC   O33000;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=ML1842;
GN   ORFNames=MLCB2492.21;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z98756; CAB11453.1; -; Genomic_DNA.
DR   EMBL; AL583923; CAC30796.1; -; Genomic_DNA.
DR   PIR; T45383; T45383.
DR   RefSeq; NP_302248.1; NC_002677.1.
DR   RefSeq; WP_010908569.1; NC_002677.1.
DR   AlphaFoldDB; O33000; -.
DR   SMR; O33000; -.
DR   STRING; 272631.ML1842; -.
DR   EnsemblBacteria; CAC30796; CAC30796; CAC30796.
DR   KEGG; mle:ML1842; -.
DR   PATRIC; fig|272631.5.peg.3492; -.
DR   Leproma; ML1842; -.
DR   eggNOG; COG0098; Bacteria.
DR   HOGENOM; CLU_065898_1_2_11; -.
DR   OMA; KNMRYFE; -.
DR   Proteomes; UP000000806; 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..217
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131549"
FT   DOMAIN          38..101
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  22614 MW;  CE1D09563DC700B4 CRC64;
     MAAQSAGLLG DSREGRSRRE GGSRGGRDRD RDGEKGNYLE RVVAINRVSK VVKGGRRFSF
     TALVIVGDGH GMVGVGYGKA KEVPAAIAKG VEEARKSFFR VPLIDGTITH PVQGEAAAGV
     VLLRPASPGT GVIAGGAVRA VLECAGVHDI LAKSLGSDNA INVVHATVAA LKLLQRPDEV
     AARRGLRSGM LPRSWDPAGV AGERSVDRPV GRVREQA
 
 
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