RS4_ACIB5
ID RS4_ACIB5 Reviewed; 208 AA.
AC B7IA15;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=AB57_3506;
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: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
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DR EMBL; CP001182; ACJ42873.1; -; Genomic_DNA.
DR RefSeq; WP_000135204.1; NC_011586.2.
DR PDB; 6V39; EM; 3.04 A; d=1-208.
DR PDB; 6V3A; EM; 2.82 A; d=1-208.
DR PDB; 6V3B; EM; 2.91 A; d=1-208.
DR PDB; 6V3E; EM; 4.40 A; d=1-208.
DR PDB; 7M4U; EM; 2.71 A; d=1-208.
DR PDB; 7M4W; EM; 2.55 A; d=1-208.
DR PDB; 7M4X; EM; 2.66 A; d=1-208.
DR PDB; 7M4Y; EM; 2.50 A; d=1-208.
DR PDB; 7M4Z; EM; 2.92 A; d=1-208.
DR PDB; 7RYF; EM; 2.65 A; d=1-208.
DR PDB; 7RYG; EM; 2.38 A; d=1-208.
DR PDB; 7RYH; EM; 2.43 A; d=1-208.
DR PDBsum; 6V39; -.
DR PDBsum; 6V3A; -.
DR PDBsum; 6V3B; -.
DR PDBsum; 6V3E; -.
DR PDBsum; 7M4U; -.
DR PDBsum; 7M4W; -.
DR PDBsum; 7M4X; -.
DR PDBsum; 7M4Y; -.
DR PDBsum; 7M4Z; -.
DR PDBsum; 7RYF; -.
DR PDBsum; 7RYG; -.
DR PDBsum; 7RYH; -.
DR AlphaFoldDB; B7IA15; -.
DR SMR; B7IA15; -.
DR IntAct; B7IA15; 1.
DR GeneID; 66395764; -.
DR KEGG; abn:AB57_3506; -.
DR HOGENOM; CLU_092403_0_2_6; -.
DR OMA; NVVFRMG; -.
DR Proteomes; UP000007094; 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 CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR005709; Ribosomal_S4_bac-type.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR PANTHER; PTHR11831:SF4; PTHR11831:SF4; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..208
FT /note="30S ribosomal protein S4"
FT /id="PRO_1000140669"
FT DOMAIN 98..160
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:7M4U"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:7M4U"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:7M4U"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:7M4U"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:7M4U"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:7M4U"
SQ SEQUENCE 208 AA; 23269 MW; C031C70963E1A84F CRC64;
MARYIGPKCK LSRREGTDLQ LKSGVKPFDV KTKKANKAPG QHGQARGGKQ SEYSLQLREK
QKVRRIYGVL ERQFSNYYKE AARVKGATGE NLLKLLESRL DNVVYRMGFG STRAEARQLV
SHRSITLNGR RVNIASIQVK AGDVIAVHEG AKQQLRIKNA IELAAQRGIP AWIEVDHSKL
EGTFKAAPDR SDLPAEINES LIVELYSK
