RS11_ACIB5
ID RS11_ACIB5 Reviewed; 128 AA.
AC B7IA16;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310};
GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; OrderedLocusNames=AB57_3507;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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}.
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DR EMBL; CP001182; ACJ42874.1; -; Genomic_DNA.
DR RefSeq; WP_001040166.1; NC_011586.2.
DR PDB; 7M4U; EM; 2.71 A; k=1-128.
DR PDBsum; 7M4U; -.
DR AlphaFoldDB; B7IA16; -.
DR SMR; B7IA16; -.
DR IntAct; B7IA16; 1.
DR GeneID; 67513074; -.
DR KEGG; abn:AB57_3507; -.
DR HOGENOM; CLU_072439_5_0_6; -.
DR OMA; KWGVAHI; -.
DR Proteomes; UP000007094; Chromosome.
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 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..128
FT /note="30S ribosomal protein S11"
FT /id="PRO_1000141041"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:7M4U"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 59..74
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:7M4U"
SQ SEQUENCE 128 AA; 13534 MW; 6A0515AF807D91BE CRC64;
MAKDTRTRKK VTRTVSEGVA HIHASFNNTI VTITDRQGNA LAWATSGGQG FRGSRKSTPF
AAQVAAEVAG KAALDYGLKN LDVLVKGPGP GRESAVRALG AVGYKINSIT DVTPIPHNGC
RPPKKRRV
