ID A0A0N9WCD7_9GAMM Unreviewed; 182 AA.
AC A0A0N9WCD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN ORFNames=AOY20_05390 {ECO:0000313|EMBL:ALH95018.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95018.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH95018.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH95018.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012808; ALH95018.1; -; Genomic_DNA.
DR RefSeq; WP_054580917.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9WCD7; -.
DR STRING; 1324350.AOY20_05390; -.
DR KEGG; aei:AOY20_05390; -.
DR OrthoDB; 9783509at2; -.
DR Proteomes; UP000064939; 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: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:UP000064939};
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 13..95
FT /note="RimM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01782"
FT DOMAIN 102..177
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
SQ SEQUENCE 182 AA; 20678 MW; A397906190F3AF87 CRC64;
MTPTQNVPED RIQIGQLRSA YGLNGWLWVY SNTEPMSNIF DYLPWYIETK AGWQIIDVKR
WKPHGKGLVV SLKGVSDRTA ADGLVGANVW ISKSQLPQAG VDEFYWSDLK GLTVLGLNDE
EQEVNLGKIH ELFETGANDV MVVRATPESI DSEERMIPWH KDVVQRVDIE AGRIYVNWGV
DY
//
