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RIMM_STAAN
ID   RIMM_STAAN              Reviewed;         167 AA.
AC   P66656; Q99UN1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014};
GN   Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; OrderedLocusNames=SA1082;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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. Probably interacts with S19. Essential for efficient processing
CC       of 16S rRNA. May be needed both before and after RbfA during the
CC       maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits
CC       but not for 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00014}.
CC   -!- SUBUNIT: Binds ribosomal protein S19. {ECO:0000255|HAMAP-
CC       Rule:MF_00014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}.
CC   -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19.
CC       {ECO:0000255|HAMAP-Rule:MF_00014}.
CC   -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP-
CC       Rule:MF_00014}.
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DR   EMBL; BA000018; BAB42334.1; -; Genomic_DNA.
DR   PIR; B89897; B89897.
DR   RefSeq; WP_001261987.1; NC_002745.2.
DR   AlphaFoldDB; P66656; -.
DR   SMR; P66656; -.
DR   EnsemblBacteria; BAB42334; BAB42334; BAB42334.
DR   KEGG; sau:SA1082; -.
DR   HOGENOM; CLU_077636_3_1_9; -.
DR   OMA; KFYFHEV; -.
DR   Proteomes; UP000000751; 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:InterPro.
DR   Gene3D; 2.40.30.60; -; 1.
DR   HAMAP; MF_00014; Ribosome_mat_RimM; 1.
DR   InterPro; IPR011961; 16S_RimM.
DR   InterPro; IPR027275; PRC-brl_dom.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   InterPro; IPR002676; RimM_N.
DR   InterPro; IPR036976; RimM_N_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   Pfam; PF05239; PRC; 1.
DR   Pfam; PF01782; RimM; 1.
DR   SUPFAM; SSF50346; SSF50346; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR02273; 16S_RimM; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Ribosome biogenesis.
FT   CHAIN           1..167
FT                   /note="Ribosome maturation factor RimM"
FT                   /id="PRO_0000163353"
FT   DOMAIN          94..165
FT                   /note="PRC barrel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00014"
SQ   SEQUENCE   167 AA;  19073 MW;  715FCD7F5708C850 CRC64;
     MRVEVGQIVN THGIKGEIKV KSNSDFTDVR FQPGQVLTVV HNNNDLEYTV KSHRVHKGLH
     MLTFEGINNI NDIEHLKGSS IYQERDHEDI VLEENEFYYS DIIGCTVFDD QETPIGRVIN
     IFETGANDVW VIKGSKEYLI PYIADVVKEV DVENKKIIIT PMEGLLD
 
 
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