RIMM_ACIAD
ID RIMM_ACIAD Reviewed; 182 AA.
AC Q6F7I0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; OrderedLocusNames=ACIAD3312;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of the protein Q6F7I0 from Acinetobacter calcoaceticus
RT AmMS 248.";
RL Submitted (JUL-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. {ECO:0000255|HAMAP-
CC Rule:MF_00014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}.
CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19.
CC {ECO:0000255|HAMAP-Rule:MF_00014}.
CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP-
CC Rule:MF_00014}.
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DR EMBL; CR543861; CAG69985.1; -; Genomic_DNA.
DR RefSeq; WP_004923846.1; NC_005966.1.
DR PDB; 2QGG; X-ray; 2.40 A; A=1-182.
DR PDBsum; 2QGG; -.
DR AlphaFoldDB; Q6F7I0; -.
DR SMR; Q6F7I0; -.
DR STRING; 62977.ACIAD3312; -.
DR EnsemblBacteria; CAG69985; CAG69985; ACIAD3312.
DR GeneID; 45235513; -.
DR KEGG; aci:ACIAD3312; -.
DR eggNOG; COG0806; Bacteria.
DR HOGENOM; CLU_077636_1_0_6; -.
DR OMA; DEFYHAD; -.
DR OrthoDB; 1497415at2; -.
DR BioCyc; ASP62977:ACIAD_RS14990-MON; -.
DR EvolutionaryTrace; Q6F7I0; -.
DR Proteomes; UP000000430; 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..182
FT /note="Ribosome maturation factor RimM"
FT /id="PRO_0000163239"
FT DOMAIN 101..182
FT /note="PRC barrel"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00014"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:2QGG"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2QGG"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2QGG"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2QGG"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2QGG"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:2QGG"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2QGG"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2QGG"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:2QGG"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2QGG"
SQ SEQUENCE 182 AA; 20818 MW; C4E1A63EC9FABEE5 CRC64;
MTPTQNVPED RIQIGQLRSA YGLNGWLWVY SNTEPMSNMF DYLPWFIETK AGWQTVDVKR
WKPHGKGLVV SLKNVSDRNA AESLIGSTIW VAKSQLPKTD VDEYYWSDLK GLTVLGLDEE
EQEVNLGQIH ELFETGANDV MVVRATADSV DAEERMIPWH KDVVQRVDLE AGRIYVNWGV
DY
