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Database: UniProt
Entry: M1WSK3_PSEP2
LinkDB: M1WSK3_PSEP2
Original site: M1WSK3_PSEP2 
ID   M1WSK3_PSEP2            Unreviewed;       206 AA.
AC   M1WSK3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
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:CCH48932.1};
GN   OrderedLocusNames=BN4_11697 {ECO:0000313|EMBL:CCH48932.1};
OS   Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS   (Desulfovibrio piezophilus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH48932.1, ECO:0000313|Proteomes:UP000011724};
RN   [1] {ECO:0000313|EMBL:CCH48932.1, ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA   Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA   Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA   Ollivier B., Dolla A.;
RT   "The first genomic and proteomic characterization of a deep-sea sulfate
RT   reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT   piezophilus.";
RL   PLoS ONE 8:e55130-e55130(2013).
RN   [2] {ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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}.
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DR   EMBL; FO203427; CCH48932.1; -; Genomic_DNA.
DR   RefSeq; WP_015414976.1; NC_020409.1.
DR   AlphaFoldDB; M1WSK3; -.
DR   STRING; 1322246.BN4_11697; -.
DR   KEGG; dpi:BN4_11697; -.
DR   PATRIC; fig|879567.3.peg.1781; -.
DR   eggNOG; COG0806; Bacteria.
DR   HOGENOM; CLU_077636_0_0_7; -.
DR   OrthoDB; 5381335at2; -.
DR   BioCyc; DPIE1322246:BN4_RS08510-MONOMER; -.
DR   Proteomes; UP000011724; 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:UP000011724};
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          11..94
FT                   /note="RimM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01782"
FT   DOMAIN          101..173
FT                   /note="PRC-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05239"
FT   REGION          176..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  23128 MW;  0885358EB82BD613 CRC64;
     MTTRRTDGFI QVGGVAKPHG IRGEFCIKSY ADSPSLFGSV AALFLQDGNK PPKPFVLRSW
     REHKGLVLLK CQGVDDRDEA EALRGFAVLV HEDDLPAPEE GQHYLYEMLG CRVRLQDGAD
     LGTLEQFFET AEQDTWVIIT DDGKEILLPA VPEFVLDVDL DEEVILVDPP EGLIDLYLNP
     EPPQKKKPRR RTSKKKPRPP KTPQAE
//
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