RS5_GEOSE
ID RS5_GEOSE Reviewed; 166 AA.
AC P02357;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=30S ribosomal protein S5;
DE Short=BS5;
DE AltName: Full=BS6;
GN Name=rpsE;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=6363400; DOI=10.1016/s0021-9258(17)43564-2;
RA Kimura M.;
RT "Proteins of the Bacillus stearothermophilus ribosome. The amino acid
RT sequences of proteins S5 and L30.";
RL J. Biol. Chem. 259:1051-1055(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1985969; DOI=10.1016/s0021-9258(17)35255-9;
RA Ramakrishnan V., Gerchman S.E.;
RT "Cloning, sequencing, and overexpression of genes for ribosomal proteins
RT from Bacillus stearothermophilus.";
RL J. Biol. Chem. 266:880-885(1991).
RN [3]
RP PROTEIN SEQUENCE OF 1-15.
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RX PubMed=4607606; DOI=10.1016/0014-5793(74)80391-1;
RA Yaguchi M., Matheson A.T., Visentin L.P.;
RT "Procaryotic ribosomal proteins: N-terminal sequence homologies and
RT structural correspondence of 30 S ribosomal proteins from Escherichia coli
RT and Bacillus stearothermophilus.";
RL FEBS Lett. 46:296-300(1974).
RN [4]
RP ISOLATION OF STREPTOMYCIN INDEPENDENT STRAINS.
RC STRAIN=799;
RX PubMed=2254291; DOI=10.1128/jb.172.12.7306-7309.1990;
RA Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T.;
RT "Isolation and characterization of Bacillus stearothermophilus 30S and 50S
RT ribosomal protein mutations.";
RL J. Bacteriol. 172:7306-7309(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=1508272; DOI=10.1038/358768a0;
RA Ramakrishnan V., White S.W.;
RT "The structure of ribosomal protein S5 reveals sites of interaction with
RT 16S rRNA.";
RL Nature 358:768-771(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9642068; DOI=10.1006/jmbi.1998.1780;
RA Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V.,
RA White S.W.;
RT "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles
RT in protein synthesis and antibiotic resistance.";
RL J. Mol. Biol. 279:873-888(1998).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000250}.
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:0000250}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 and S8
CC (By similarity). {ECO:0000250}.
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:0000305}.
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DR EMBL; M57621; AAA22699.1; -; Genomic_DNA.
DR PIR; A02708; R3BS5F.
DR RefSeq; WP_033017242.1; NZ_RCTK01000011.1.
DR PDB; 1DV4; X-ray; 4.50 A; E=4-148.
DR PDB; 1PKP; X-ray; 2.80 A; A=1-150.
DR PDBsum; 1DV4; -.
DR PDBsum; 1PKP; -.
DR AlphaFoldDB; P02357; -.
DR SMR; P02357; -.
DR IntAct; P02357; 1.
DR MINT; P02357; -.
DR GeneID; 58573179; -.
DR EvolutionaryTrace; P02357; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Direct protein sequencing;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..166
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131469"
FT DOMAIN 11..74
FT /note="S5 DRBM"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 42..55
FT /evidence="ECO:0007829|PDB:1PKP"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1PKP"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:1PKP"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1PKP"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:1PKP"
SQ SEQUENCE 166 AA; 17628 MW; 774E82A2ED1D8EC5 CRC64;
MRRINPNKLE LEERVVAVNR VAKVVKGGRR LRFSALVVVG DKNGHVGFGT GKAQEVPEAI
RKAIEDAKKN LIEVPIVGTT IPHEVIGHFG AGEIILKPAS EGTGVIAGGP ARAVLELAGI
SDILSKSIGS NTPINMVRAT FDGLKQLKRA EDVAKLRGKT VEELLG
