RS5_UREU1
ID RS5_UREU1 Reviewed; 203 AA.
AC B5ZB57;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=UUR10_0243;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001184; ACI59998.1; -; Genomic_DNA.
DR RefSeq; WP_004026225.1; NC_011374.1.
DR AlphaFoldDB; B5ZB57; -.
DR SMR; B5ZB57; -.
DR STRING; 565575.UUR10_0243; -.
DR EnsemblBacteria; ACI59998; ACI59998; UUR10_0243.
DR GeneID; 45015792; -.
DR KEGG; uue:UUR10_0243; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_1_14; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 1505038at2; -.
DR Proteomes; UP000002018; 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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..203
FT /note="30S ribosomal protein S5"
FT /id="PRO_1000140903"
FT DOMAIN 49..112
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22177 MW; 0C7C3CC7A131E6D6 CRC64;
MENNVKKETI VDSEKVEKQQ PVTAPVVNKK ENTQPKAKTF KRETTTSNFE ERVVKIKRIS
KTTKGGRMMR FSALVVIGDK NGTVGFGMGK SIEVPDAIKK AIKNANNNLI KVKQTKKGSI
YHDVNGRHGA AKVMLLPAPE GTGIIAGGPV RAVVELAGFT DIYTKSRGAN APMNVIRATI
NGLLQQLTPQ EIARLRDKSL KEL
