ID A0A3S0VQ97_9BACI Unreviewed; 172 AA.
AC A0A3S0VQ97;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=Ribosome maturation factor RimM {ECO:0000256|HAMAP-Rule:MF_00014};
GN Name=rimM {ECO:0000256|HAMAP-Rule:MF_00014,
GN ECO:0000313|EMBL:RUQ30421.1};
GN ORFNames=ELQ35_08775 {ECO:0000313|EMBL:RUQ30421.1};
OS Peribacillus cavernae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ30421.1, ECO:0000313|Proteomes:UP000267430};
RN [1] {ECO:0000313|EMBL:RUQ30421.1, ECO:0000313|Proteomes:UP000267430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L5 {ECO:0000313|EMBL:RUQ30421.1,
RC ECO:0000313|Proteomes:UP000267430};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (DEC-2018) 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. 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:RUQ30421.1}.
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DR EMBL; RYZZ01000007; RUQ30421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0VQ97; -.
DR OrthoDB; 9810331at2; -.
DR Proteomes; UP000267430; 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:UP000267430};
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 7..91
FT /note="RimM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01782"
FT DOMAIN 97..171
FT /note="PRC-barrel"
FT /evidence="ECO:0000259|Pfam:PF05239"
SQ SEQUENCE 172 AA; 19514 MW; 62828A1778EBD432 CRC64;
MEKWFNVGKI VNTHGIMGEV RVISRTDFQE ERYKEGNTLF LFIENENEPI ELKITSHRTH
KNFDLLTFEN YTNVNMSESL KGGLLKVPES QLGKLDEGEY YFHEIIGCTV YTDEGGEIGK
VREVLTPGAN DVWVIKGMGG KDILIPYIDG IVSEVDIESK KIIITPMEGL LD
//