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RS3_ACIB5
ID   RS3_ACIB5               Reviewed;         250 AA.
AC   B7IA33;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309};
GN   Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=AB57_3524;
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: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-
CC       Rule:MF_01309}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01309}.
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DR   EMBL; CP001182; ACJ42891.1; -; Genomic_DNA.
DR   PDB; 7M4U; EM; 2.71 A; c=1-250.
DR   PDBsum; 7M4U; -.
DR   AlphaFoldDB; B7IA33; -.
DR   SMR; B7IA33; -.
DR   IntAct; B7IA33; 1.
DR   KEGG; abn:AB57_3524; -.
DR   HOGENOM; CLU_058591_0_2_6; -.
DR   OMA; KTNPIGN; -.
DR   Proteomes; UP000007094; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
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; 3.30.1140.32; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
DR   TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..250
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_1000140913"
FT   DOMAIN          39..107
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01309"
FT   REGION          215..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   TURN            12..15
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           29..46
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          61..71
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           73..77
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           82..94
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           130..143
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          147..156
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          164..171
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          180..191
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   STRAND          194..206
FT                   /evidence="ECO:0007829|PDB:7M4U"
FT   HELIX           210..214
FT                   /evidence="ECO:0007829|PDB:7M4U"
SQ   SEQUENCE   250 AA;  27907 MW;  3FCFB1D55E9BA0D2 CRC64;
     MGQKVHPIGI RLGVVKRHNA NWYANPKQYA EYLLKDLQVR EFLTKNLKNA MVSNILIERP
     SGAAKVTIST ARPGIVIGKK GEDIEKLQRE LTNIMGVPAQ VSINEIDRPD LDARLVAEAI
     ASQLEKRVMF RRAMKRAVQN TMRAGAKGIK VEVSGRLGGA EIARTEWYRE GRVPLHTLRA
     DIDYATMRAE TTYGTIGVKV WIFRGEILGG MKQVMNPAPA EERPAKRGRG RGEGQERRGR
     RGDRAADKGE
 
 
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