RRF_EHRCR
ID RRF_EHRCR Reviewed; 185 AA.
AC Q2GHJ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Ribosome-recycling factor {ECO:0000255|HAMAP-Rule:MF_00040};
DE Short=RRF {ECO:0000255|HAMAP-Rule:MF_00040};
DE AltName: Full=Ribosome-releasing factor {ECO:0000255|HAMAP-Rule:MF_00040};
GN Name=frr {ECO:0000255|HAMAP-Rule:MF_00040}; OrderedLocusNames=ECH_0267;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: Responsible for the release of ribosomes from messenger RNA
CC at the termination of protein biosynthesis. May increase the efficiency
CC of translation by recycling ribosomes from one round of translation to
CC another. {ECO:0000255|HAMAP-Rule:MF_00040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00040}.
CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP-
CC Rule:MF_00040}.
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DR EMBL; CP000236; ABD45378.1; -; Genomic_DNA.
DR RefSeq; WP_011452494.1; NC_007799.1.
DR PDB; 6VUD; X-ray; 2.35 A; A/B=1-185.
DR PDBsum; 6VUD; -.
DR AlphaFoldDB; Q2GHJ5; -.
DR SMR; Q2GHJ5; -.
DR STRING; 205920.ECH_0267; -.
DR EnsemblBacteria; ABD45378; ABD45378; ECH_0267.
DR KEGG; ech:ECH_0267; -.
DR eggNOG; COG0233; Bacteria.
DR HOGENOM; CLU_073981_2_1_5; -.
DR OMA; FNPMNNG; -.
DR OrthoDB; 1674344at2; -.
DR Proteomes; UP000008320; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006415; P:translational termination; IEA:UniProtKB-UniRule.
DR CDD; cd00520; RRF; 1.
DR Gene3D; 1.10.132.20; -; 1.
DR HAMAP; MF_00040; RRF; 1.
DR InterPro; IPR002661; Ribosome_recyc_fac.
DR InterPro; IPR023584; Ribosome_recyc_fac_dom.
DR InterPro; IPR036191; RRF_sf.
DR PANTHER; PTHR20982; PTHR20982; 1.
DR Pfam; PF01765; RRF; 1.
DR SUPFAM; SSF55194; SSF55194; 1.
DR TIGRFAMs; TIGR00496; frr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein biosynthesis; Reference proteome.
FT CHAIN 1..185
FT /note="Ribosome-recycling factor"
FT /id="PRO_1000003160"
FT HELIX 2..25
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6VUD"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 107..144
FT /evidence="ECO:0007829|PDB:6VUD"
FT HELIX 150..183
FT /evidence="ECO:0007829|PDB:6VUD"
SQ SEQUENCE 185 AA; 20710 MW; 3460607890F71097 CRC64;
MISEVKQDAK SRMEKSLSVY LSDIDGIRTG RARTSVLNGI VVETYGGRVK LNTISSVSVS
DNKTLMIKVW DSNNIGAIKT AIMNSNLGFG ISCEATTIRL TVPDMTQDMR KNLVKLLGKI
SEDCRVSIRN IRRDIMDRLK VMQDSKEISE DDLRVAGVEI QKITDDIMKK VNDAFTSKEK
ELLHV