RS5_PICTO
ID RS5_PICTO Reviewed; 221 AA.
AC Q6L1A7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=PTO0660;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4.
CC {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; AE017261; AAT43245.1; -; Genomic_DNA.
DR RefSeq; WP_011177461.1; NC_005877.1.
DR AlphaFoldDB; Q6L1A7; -.
DR SMR; Q6L1A7; -.
DR STRING; 263820.PTO0660; -.
DR EnsemblBacteria; AAT43245; AAT43245; PTO0660.
DR GeneID; 2845391; -.
DR KEGG; pto:PTO0660; -.
DR PATRIC; fig|263820.9.peg.693; -.
DR eggNOG; arCOG04087; Archaea.
DR HOGENOM; CLU_065898_0_1_2; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 60954at2157; -.
DR Proteomes; UP000000438; 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_A; Ribosomal_S5_A; 1.
DR InterPro; IPR000851; Ribosomal_S5.
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; IPR005711; Ribosomal_S5_euk/arc.
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; TIGR01020; uS5_euk_arch; 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..221
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131654"
FT DOMAIN 46..109
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 221 AA; 23602 MW; 82FC8C43E02EFC12 CRC64;
MDEEWTPRTE LGRLVANGEI KTISEALHSK LPLKEYQIVD YLIPDLKDEV INIERAQRMT
DSGRRMNYSI TAVVGNGNGY VGVGRGKAKE AAPAIKKAID NAKLNIIEIK RGCGSWECGC
GKPHTLPFLV NGKSGSVSVT LKPAPQGVGL AVGDVVKVIL RMAGIDDAWG FAAGHTKTTV
NYALATFDAL KKTVSIKINP KINLSTPIYV GGIGNAGSNK D