RS7_THEMA
ID RS7_THEMA Reviewed; 155 AA.
AC P38526;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480};
GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=TM_1504;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-155.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=1920450; DOI=10.1007/bf02193628;
RA Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.;
RT "Phylogenetic depth of Thermotoga maritima inferred from analysis of the
RT fus gene: amino acid sequence of elongation factor G and organization of
RT the Thermotoga str operon.";
RL J. Mol. Evol. 33:142-151(1991).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the head domain of the 30S
CC subunit. Is located at the subunit interface close to the decoding
CC center, probably blocks exit of the E-site tRNA. {ECO:0000255|HAMAP-
CC Rule:MF_00480}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 and
CC S11. {ECO:0000255|HAMAP-Rule:MF_00480}.
CC -!- INTERACTION:
CC P38526; Q9WZF8: tig; NbExp=5; IntAct=EBI-2463521, EBI-2463534;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC {ECO:0000255|HAMAP-Rule:MF_00480}.
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DR EMBL; AE000512; AAD36571.1; -; Genomic_DNA.
DR EMBL; S57688; AAB19928.1; -; Genomic_DNA.
DR PIR; A72244; A72244.
DR RefSeq; NP_229304.1; NC_000853.1.
DR RefSeq; WP_004081843.1; NZ_CP011107.1.
DR PDB; 3GTY; X-ray; 3.40 A; S=9-155.
DR PDBsum; 3GTY; -.
DR AlphaFoldDB; P38526; -.
DR SMR; P38526; -.
DR IntAct; P38526; 1.
DR STRING; 243274.THEMA_06780; -.
DR DNASU; 897994; -.
DR EnsemblBacteria; AAD36571; AAD36571; TM_1504.
DR KEGG; tma:TM1504; -.
DR eggNOG; COG0049; Bacteria.
DR InParanoid; P38526; -.
DR OMA; NVMPHVE; -.
DR OrthoDB; 1540940at2; -.
DR EvolutionaryTrace; P38526; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 1.10.455.10; -; 1.
DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR InterPro; IPR000235; Ribosomal_S5/S7.
DR InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR InterPro; IPR020606; Ribosomal_S7_CS.
DR InterPro; IPR023798; Ribosomal_S7_dom.
DR InterPro; IPR036823; Ribosomal_S7_dom_sf.
DR PANTHER; PTHR11205; PTHR11205; 1.
DR Pfam; PF00177; Ribosomal_S7; 1.
DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR SUPFAM; SSF47973; SSF47973; 1.
DR TIGRFAMs; TIGR01029; rpsG_bact; 1.
DR PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..155
FT /note="30S ribosomal protein S7"
FT /id="PRO_0000124367"
FT CONFLICT 105
FT /note="E -> Q (in Ref. 2; AAB19928)"
FT /evidence="ECO:0000305"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3GTY"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:3GTY"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3GTY"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3GTY"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:3GTY"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:3GTY"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3GTY"
SQ SEQUENCE 155 AA; 17988 MW; DB52CB3AF8F942E1 CRC64;
MRRRRAEKRQ IPPDPVFGDV LVAKLINRVM WDGKKTIAQK IVYGAFDIIR EKTKKDPLEV
FRQAVENVKP VLEVRPRRVG GATYQVPIEV QEPRRTSLAL RWIVEAARAK KGRPMKEKLA
EEIIAAYNNT GTAIKKKEDT HRMAEANRAF AHYRW
