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RBFA_CORK4
ID   RBFA_CORK4              Reviewed;         155 AA.
AC   C4LJ81;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003};
GN   Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; OrderedLocusNames=ckrop_1141;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
CC   -!- FUNCTION: One of several proteins that assist in the late maturation
CC       steps of the functional core of the 30S ribosomal subunit. Associates
CC       with free 30S ribosomal subunits (but not with 30S subunits that are
CC       part of 70S ribosomes or polysomes). Required for efficient processing
CC       of 16S rRNA. May interact with the 5'-terminal helix region of 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SUBUNIT: Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal
CC       subunits or 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003}.
CC   -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00003}.
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DR   EMBL; CP001620; ACR17886.1; -; Genomic_DNA.
DR   RefSeq; WP_012731773.1; NC_012704.1.
DR   AlphaFoldDB; C4LJ81; -.
DR   SMR; C4LJ81; -.
DR   STRING; 645127.ckrop_1141; -.
DR   EnsemblBacteria; ACR17886; ACR17886; ckrop_1141.
DR   KEGG; ckp:ckrop_1141; -.
DR   eggNOG; COG0858; Bacteria.
DR   HOGENOM; CLU_089475_0_0_11; -.
DR   OMA; GDLQHCK; -.
DR   OrthoDB; 1971380at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00003; RbfA; 1.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR000238; RbfA.
DR   InterPro; IPR023799; RbfA_dom_sf.
DR   InterPro; IPR020053; Ribosome-bd_factorA_CS.
DR   PANTHER; PTHR33515; PTHR33515; 1.
DR   Pfam; PF02033; RBFA; 1.
DR   SUPFAM; SSF89919; SSF89919; 1.
DR   TIGRFAMs; TIGR00082; rbfA; 1.
DR   PROSITE; PS01319; RBFA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..155
FT                   /note="Ribosome-binding factor A"
FT                   /id="PRO_1000201626"
FT   REGION          116..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   155 AA;  17246 MW;  5723FE1708820A5F CRC64;
     MADRARAARM AKRIQTIVAN TIEHSVKDRR LELVTITDTQ LTGDLHDATV FYTVRGRTLD
     EEPDREQAAE ALHRARGQLR KAVGDQLGVR FTPTLTFTLD TVPETSARLE ELLAQARQRD
     QEVARQAEGA TPAGDANPYK TSPHEGRPES EADGW
 
 
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