ID A0A1Q4W9I7_9ACTN Unreviewed; 184 AA.
AC A0A1Q4W9I7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN ORFNames=A6A06_36980 {ECO:0000313|EMBL:OKI06762.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI06762.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI06762.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI06762.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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. Essential for efficient processing of 16S rRNA. May be needed
CC both before and after RbfA during the maturation of 16S rRNA. It has
CC affinity for free ribosomal 30S subunits but not for 70S ribosomes.
CC {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- SUBUNIT: Binds ribosomal protein uS19. {ECO:0000256|HAMAP-
CC Rule:MF_00014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein uS19.
CC {ECO:0000256|HAMAP-Rule:MF_00014}.
CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000256|HAMAP-
CC Rule:MF_00014}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKI06762.1}.
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DR EMBL; LWKZ01000006; OKI06762.1; -; Genomic_DNA.
DR RefSeq; WP_073760852.1; NZ_LWKZ01000006.1.
DR AlphaFoldDB; A0A1Q4W9I7; -.
DR STRING; 1718985.A6A06_36980; -.
DR OrthoDB; 5381335at2; -.
DR Proteomes; UP000185893; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR Gene3D; 2.30.30.240; PRC-barrel domain; 1.
DR Gene3D; 2.40.30.60; RimM; 1.
DR HAMAP; MF_00014; Ribosome_mat_RimM; 1.
DR InterPro; IPR027275; PRC-brl_dom.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR InterPro; IPR011961; RimM.
DR InterPro; IPR002676; RimM_N.
DR InterPro; IPR036976; RimM_N_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR02273; 16S_RimM; 1.
DR PANTHER; PTHR33692; RIBOSOME MATURATION FACTOR RIMM; 1.
DR PANTHER; PTHR33692:SF1; RIBOSOME MATURATION FACTOR RIMM; 1.
DR Pfam; PF05239; PRC; 1.
DR Pfam; PF01782; RimM; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00014};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00014};
KW Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00014};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00014}.
FT DOMAIN 4..83
FT /note="RimM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01782"
FT DOMAIN 94..167
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
FT REGION 160..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 184 AA; 20023 MW; BB3B611E36061468 CRC64;
MQLVVARIGR AHGIKGEVTV EVRTDEPELR LAPGAVLATD PPATGPLTIE TGRVHSGRLL
LRFEGVRDRT GAEALRNTLL IAEIDPEEVP EDPEEYYDHQ LIDLDVVTTD GKEIGRIAEV
SHLPYQDLLI VRRPDGDEVM IPFVSEIVPE IDLAEQKAVV DPPPGLLDDS QAEVASARDA
GEDA
//