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RS15_GEOSE
ID   RS15_GEOSE              Reviewed;          89 AA.
AC   P05766;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343};
DE   AltName: Full=BS18;
GN   Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-89.
RX   PubMed=1764513; DOI=10.1016/0300-9084(91)90045-3;
RA   Arndt E., Scholzen T., Kromer W., Hatakeyama T., Kimura M.;
RT   "Primary structures of ribosomal proteins from the archaebacterium
RT   Halobacterium marismortui and the eubacterium Bacillus
RT   stearothermophilus.";
RL   Biochimie 73:657-668(1991).
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 46.
RX   PubMed=9562554; DOI=10.1016/s0969-2126(98)00045-8;
RA   Clemons W.M. Jr., Davies C., White S.W., Ramakrishnan V.;
RT   "Conformational variability of the N-terminal helix in the structure of
RT   ribosomal protein S15.";
RL   Structure 6:429-438(1998).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it helps nucleate assembly of the platform of the 30S
CC       subunit by binding and bridging several RNA helices of the 16S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S rRNA of
CC       the 50S subunit in the ribosome. {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the 50S
CC       subunit in the 70S ribosome, contacting the 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01343}.
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DR   RefSeq; WP_033016867.1; NZ_RCTK01000001.1.
DR   PDB; 1A32; X-ray; 2.10 A; A=2-89.
DR   PDBsum; 1A32; -.
DR   AlphaFoldDB; P05766; -.
DR   SMR; P05766; -.
DR   IntAct; P05766; 6.
DR   GeneID; 58572351; -.
DR   EvolutionaryTrace; P05766; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR   HAMAP; MF_01343_B; Ribosomal_S15_B; 1.
DR   InterPro; IPR000589; Ribosomal_S15.
DR   InterPro; IPR005290; Ribosomal_S15_bac-type.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   PANTHER; PTHR23321; PTHR23321; 1.
DR   Pfam; PF00312; Ribosomal_S15; 1.
DR   SMART; SM01387; Ribosomal_S15; 1.
DR   SUPFAM; SSF47060; SSF47060; 1.
DR   TIGRFAMs; TIGR00952; S15_bact; 1.
DR   PROSITE; PS00362; RIBOSOMAL_S15; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1764513,
FT                   ECO:0000269|PubMed:4607606"
FT   CHAIN           2..89
FT                   /note="30S ribosomal protein S15"
FT                   /id="PRO_0000115380"
FT   CONFLICT        13..14
FT                   /note="EQ -> GE (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="H -> R (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..14
FT                   /evidence="ECO:0007829|PDB:1A32"
FT   HELIX           25..45
FT                   /evidence="ECO:0007829|PDB:1A32"
FT   HELIX           51..73
FT                   /evidence="ECO:0007829|PDB:1A32"
FT   HELIX           75..85
FT                   /evidence="ECO:0007829|PDB:1A32"
SQ   SEQUENCE   89 AA;  10691 MW;  B0387CC4B04DE000 CRC64;
     MALTQERKRE IIEQFKVHEN DTGSPEVQIA ILTEQINNLN EHLRVHKKDH HSRRGLLKMV
     GKRRRLLAYL RNKDVARYRE IVEKLGLRR
 
 
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