RS5_METMA
ID RS5_METMA Reviewed; 209 AA.
AC Q8PV30;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=MM_2144;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31840.1; -; Genomic_DNA.
DR RefSeq; WP_011034075.1; NC_003901.1.
DR AlphaFoldDB; Q8PV30; -.
DR SMR; Q8PV30; -.
DR STRING; 192952.MM_2144; -.
DR EnsemblBacteria; AAM31840; AAM31840; MM_2144.
DR GeneID; 44088222; -.
DR GeneID; 66136371; -.
DR KEGG; mma:MM_2144; -.
DR PATRIC; fig|192952.21.peg.2458; -.
DR eggNOG; arCOG04087; Archaea.
DR HOGENOM; CLU_065898_0_1_2; -.
DR OMA; KRGCGSW; -.
DR Proteomes; UP000000595; 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..209
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131650"
FT DOMAIN 48..111
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 209 AA; 22718 MW; 3DCEE62A1F1BFF0C CRC64;
MAFDQDWVPK TRLGKLVVEG QVASMDEAIK SGLPIREPQI IDMLLPDLED EVLDINMVQR
MTDSGRRVKF RATVIVGNRN GYVGLGQAKD VQVGPAIRKA IDAAKLNITY IRRGCGSWEC
ACGLPHTVPY EVTGKAGSVS VTLIPAPRGL GIAAGNTATK VLEKAGIKDV WTKTFGTTRS
TLNFAKATYD ALNQVNVVRL PVYYGKEEI
