RS11_GEOSE
ID RS11_GEOSE Reviewed; 129 AA.
AC P10789;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
DE Short=BS11;
GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP PROTEIN SEQUENCE OF 2-129.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=3191988; DOI=10.1016/0014-5793(88)80332-6;
RA Kimura M., Kimura J., Hatakeyama T.;
RT "Amino acid sequences of ribosomal proteins S11 from Bacillus
RT stearothermophilus and S19 from Halobacterium marismortui. Comparison of
RT the ribosomal protein S11 family.";
RL FEBS Lett. 240:15-20(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-16.
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).
CC -!- FUNCTION: Located on the platform of the 30S subunit, it bridges
CC several disparate RNA helices of the 16S rRNA. Forms part of the Shine-
CC Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with proteins S7
CC and S18. Binds to IF-3. {ECO:0000255|HAMAP-Rule:MF_01310}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000255|HAMAP-Rule:MF_01310}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S01781; R3BS11.
DR AlphaFoldDB; P10789; -.
DR SMR; P10789; -.
DR PRIDE; P10789; -.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR019981; Ribosomal_S11_bac-type.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR TIGRFAMs; TIGR03632; uS11_bact; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3191988,
FT ECO:0000269|PubMed:4607606"
FT CHAIN 2..129
FT /note="30S ribosomal protein S11"
FT /id="PRO_0000123105"
SQ SEQUENCE 129 AA; 13811 MW; 9958C8F647FC7A00 CRC64;
MARRTNTRKR RVRKNIDTGI AHIRSTFNNT IVTITDVHGN ALAWASAGSL GFKGSRKSTP
FAAQMAAEAA AKASMEHGMK TVEVNVKGPG AGREAAIRAL QAAGLEITAI KDVTPIPHDG
CRPPKRRRV