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RS5_MYCS2
ID   RS5_MYCS2               Reviewed;         214 AA.
AC   A0QSG6; I7G5Q3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307};
GN   OrderedLocusNames=MSMEG_1472, MSMEI_1436;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK71824.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37909.1; -; Genomic_DNA.
DR   RefSeq; WP_003892859.1; NZ_SIJM01000016.1.
DR   RefSeq; YP_885854.1; NC_008596.1.
DR   PDB; 5O5J; EM; 3.45 A; E=1-214.
DR   PDB; 5O61; EM; 3.31 A; BE=1-214.
DR   PDB; 5XYU; EM; 3.45 A; E=1-214.
DR   PDB; 5ZEB; EM; 3.40 A; e=1-214.
DR   PDB; 5ZEP; EM; 3.40 A; e=1-214.
DR   PDB; 5ZEU; EM; 3.70 A; e=1-214.
DR   PDB; 6DZI; EM; 3.46 A; m=35-214.
DR   PDB; 6DZK; EM; 3.60 A; E=2-214.
DR   PDBsum; 5O5J; -.
DR   PDBsum; 5O61; -.
DR   PDBsum; 5XYU; -.
DR   PDBsum; 5ZEB; -.
DR   PDBsum; 5ZEP; -.
DR   PDBsum; 5ZEU; -.
DR   PDBsum; 6DZI; -.
DR   PDBsum; 6DZK; -.
DR   AlphaFoldDB; A0QSG6; -.
DR   SMR; A0QSG6; -.
DR   IntAct; A0QSG6; 2.
DR   STRING; 246196.MSMEI_1436; -.
DR   PRIDE; A0QSG6; -.
DR   EnsemblBacteria; ABK71824; ABK71824; MSMEG_1472.
DR   EnsemblBacteria; AFP37909; AFP37909; MSMEI_1436.
DR   GeneID; 66732929; -.
DR   KEGG; msg:MSMEI_1436; -.
DR   KEGG; msm:MSMEG_1472; -.
DR   PATRIC; fig|246196.19.peg.1457; -.
DR   eggNOG; COG0098; Bacteria.
DR   OMA; KRGCGSW; -.
DR   OrthoDB; 1505038at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:18955433"
FT   CHAIN           2..214
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_1000086029"
FT   DOMAIN          36..99
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:5O5J"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           134..143
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           158..169
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           175..181
FT                   /evidence="ECO:0007829|PDB:5XYU"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:5O5J"
FT   HELIX           192..213
FT                   /evidence="ECO:0007829|PDB:5O5J"
SQ   SEQUENCE   214 AA;  21911 MW;  776D6119907F713C CRC64;
     MAEQAGAGSA QDNRGGRGRR DDRGGRGRDG GDKSNYIERV VSINRVSKVV KGGRRFSFTA
     LVIVGDGKGM VGVGYGKAKE VPAAIAKGVE EARKNFFRVP LIGSTITHPV QGEAAAGVVM
     LRPASPGTGV IAGGAARAVL ECAGVHDILA KSLGSDNAIN VVHATVAALK LLQRPEEVAA
     RRGLPIEDVA PAGMLKARRE SEALAAAAAR EGSA
 
 
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