RIMM_THET8
ID RIMM_THET8 Reviewed; 162 AA.
AC Q5SJH5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; OrderedLocusNames=TTHA1033;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP STRUCTURE BY NMR OF 1-85, AND INTERACTION WITH S19.
RX PubMed=17616598; DOI=10.1128/jb.00024-07;
RA Suzuki S., Tatsuguchi A., Matsumoto E., Kawazoe M., Kaminishi T.,
RA Shirouzu M., Muto Y., Takemoto C., Yokoyama S.;
RT "Structural characterization of the ribosome maturation protein, RimM.";
RL J. Bacteriol. 189:6397-6406(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of 16s ribosomal RNA processing protein RimM from
RT Thermus thermophilus HB8.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: An accessory protein needed during the final step in the
CC assembly of 30S ribosomal subunit, possibly for assembly of the head
CC region. Probably interacts with S19. Essential for efficient processing
CC of 16S rRNA. May be needed both before and after RbfA during the
CC maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits
CC but not for 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00014}.
CC -!- SUBUNIT: Binds ribosomal protein S19.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}.
CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19.
CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP-
CC Rule:MF_00014}.
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DR EMBL; AP008226; BAD70856.1; -; Genomic_DNA.
DR RefSeq; WP_011228392.1; NC_006461.1.
DR RefSeq; YP_144299.1; NC_006461.1.
DR PDB; 2DOG; NMR; -; A=1-85.
DR PDB; 2DYI; X-ray; 2.00 A; A=1-162.
DR PDB; 3A1P; X-ray; 2.30 A; A/C=1-162.
DR PDBsum; 2DOG; -.
DR PDBsum; 2DYI; -.
DR PDBsum; 3A1P; -.
DR AlphaFoldDB; Q5SJH5; -.
DR BMRB; Q5SJH5; -.
DR SMR; Q5SJH5; -.
DR STRING; 300852.55772415; -.
DR EnsemblBacteria; BAD70856; BAD70856; BAD70856.
DR GeneID; 3170094; -.
DR KEGG; ttj:TTHA1033; -.
DR PATRIC; fig|300852.9.peg.1013; -.
DR eggNOG; COG0806; Bacteria.
DR HOGENOM; CLU_077636_0_1_0; -.
DR OMA; YYYHELR; -.
DR PhylomeDB; Q5SJH5; -.
DR EvolutionaryTrace; Q5SJH5; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR Gene3D; 2.40.30.60; -; 1.
DR HAMAP; MF_00014; Ribosome_mat_RimM; 1.
DR InterPro; IPR011961; 16S_RimM.
DR InterPro; IPR027275; PRC-brl_dom.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR InterPro; IPR002676; RimM_N.
DR InterPro; IPR036976; RimM_N_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF05239; PRC; 1.
DR Pfam; PF01782; RimM; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR02273; 16S_RimM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..162
FT /note="Ribosome maturation factor RimM"
FT /id="PRO_0000163380"
FT DOMAIN 86..160
FT /note="PRC barrel"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00014"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2DYI"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2DYI"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2DYI"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:2DYI"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2DYI"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2DYI"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2DYI"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2DYI"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2DYI"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2DYI"
SQ SEQUENCE 162 AA; 18073 MW; E3ABCD7DD3430DF8 CRC64;
MRLVEIGRFG APYALKGGLR FRGEPVVLHL ERVYVEGHGW RAIEDLYRVG EELVVHLAGV
TDRTLAEALV GLRVYAEVAD LPPLEEGRYY YFALIGLPVY VEGRQVGEVV DILDAGAQDV
LIIRGVGERL RDRAERLVPL QAPYVRVEEG SIHVDPIPGL FD
