ID A0A1F4K418_9BURK Unreviewed; 187 AA.
AC A0A1F4K418;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN ORFNames=A3F78_06425 {ECO:0000313|EMBL:OGB29443.1};
OS Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB29443.1, ECO:0000313|Proteomes:UP000178940};
RN [1] {ECO:0000313|EMBL:OGB29443.1, ECO:0000313|Proteomes:UP000178940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGB29443.1}.
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DR EMBL; MESI01000107; OGB29443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4K418; -.
DR STRING; 1797566.A3F78_06425; -.
DR Proteomes; UP000178940; 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 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 16..104
FT /note="RimM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01782"
FT DOMAIN 112..182
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
SQ SEQUENCE 187 AA; 20783 MW; 4477041E5D7EA17B CRC64;
MLTGLEPADM PADAVEVGRI ADAWGIKGWF KVLPHSADPE AIFSSKRWFL LPSDRGVKAF
TGVAKLAVKE AKEHSGTVVA CAHGVDDRTS AEALRGVRIF ISRSSFPTAG DDEYYWVDLI
GLEVFNRENE ALGTVRELLS TGPQTVLVME YLHEGKIQDR MIPFVSVYVD NVDLKARRIL
VDWQADY
//
