ID   RIMM_CLOBA              Reviewed;         165 AA.
AC   B2V4E4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014};
GN   Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; OrderedLocusNames=CLH_1199;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001078; ACD51918.1; -; Genomic_DNA.
DR   RefSeq; WP_012450174.1; NC_010723.1.
DR   AlphaFoldDB; B2V4E4; -.
DR   SMR; B2V4E4; -.
DR   KEGG; cbt:CLH_1199; -.
DR   HOGENOM; CLU_077636_3_2_9; -.
DR   OMA; DEFYHAD; -.
DR   OrthoDB; 1497415at2; -.
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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Ribosome biogenesis.
FT   CHAIN           1..165
FT                   /note="Ribosome maturation factor RimM"
FT                   /id="PRO_1000089492"
FT   DOMAIN          89..161
FT                   /note="PRC barrel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00014"
SQ   SEQUENCE   165 AA;  19193 MW;  9113B6E1FF3345E3 CRC64;
     MEEIFKIGQI VNTHGIKGEV KVYPLTEDVN KFKKLKTVLI DGEHRNIQSV KFQKDRVILK
     IEGIDTMNDA ETYKQKYIEI FRSNAPELEA DTHYIVDLIG CMVYDADNME LGKIFDVIST
     PSNDVYWIKQ PKELLIPVLK DIVLDIDIEN KKIVVKPVRQ WQDED