Signal recognition particle protein

Name	Signal recognition particle protein
Synonyms	Fifty-four homolog
Gene Name	ffh
Organism	Thermus aquaticus
Amino acid sequence	>lcl\|BSEQ0011279\|Signal recognition particle protein MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVARDFVERVREEAL GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGDVASL AEKVRAAGLEAEAPKSAKELSLEDFLKQMQNLKRLGPFSEILGLLPGVPQGLKVDEKAIK RLEAIVLSMTPEERKDPRILNGSRRKRIAKGSGTSVQEVNRFIKAFEEMKALMKSLEKKK GRGLMGMFRR
Number of residues	None
Molecular Weight	47355.705
Theoretical pI	10.17
GO Classification	Functions GTP binding GTPase activity 7S RNA binding Processes SRP-dependent cotranslational protein targeting to membrane Components signal recognition particle
General Function	Gtpase activity
Specific Function	Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	O07347
UniProtKB Entry Name
Cellular Location	Cytoplasm
Gene sequence	>lcl\|BSEQ0003552\|1293 bp ATGTTCCAACAGCTTTCGGCGCGACTGCAAGAGGCCATCGGCCGCCTTAGGGGGCGGGGC CGGATCACCGAGGAGGACCTGAAGGCCACCCTCAGGGAGATCCGCCGGGCCCTCATGGAC GCCGATGTCAACCTGGAGGTGGCCCGGGACTTCGTGGAGCGGGTGCGGGAGGAGGCCTTG GGGAAGCAGGTCCTGGAGAGCCTCACCCCCGCCGAGGTGATCCTGGCCACCGTCTACGAG GCCCTCAAGGAGGCCCTGGGGGGCGAGGCCAGGCTCCCTGTCCTCAAGGACAGGAACCTC TGGTTCCTGGTGGGCCTCCAGGGCTCCGGCAAGACCACCACCGCCGCCAAGCTGGCCCTC TACTACAAGGGCAAGGGGAGGAGGCCCCTCTTGGTGGCCGCCGACACCCAGAGGCCCGCC GCCAGGGAGCAACTAAGGCTTCTGGGCGAGAAGGTGGGCGTGCCCGTGCTGGAGGTGATG GACGGGGAGTCCCCTGAGTCCATCCGCCGCCGGGTGGAGGAGAAGGCCCGCCTCGAGGCC CGGGACCTGATCCTGGTGGACACCGCCGGCCGCCTGCAGATTGACGAGCCCCTCATGGGG GAGCTGGCCCGCCTCAAGGAGGTCCTTGGCCCGGACGAGGTTCTCCTGGTCCTGGACGCC ATGACCGGGCAGGAAGCCCTTTCCGTGGCCAGGGCCTTTGACGAGAAGGTGGGGGTCACG GGCCTCGTCCTCACCAAGCTGGACGGGGATGCCCGGGGCGGGGCGGCCCTTTCCGCCCGC CACGTGACGGGCAAGCCCATCTACTTCGCCGGGGTTTCCGAGAAGCCGGAGGGCCTGGAG CCCTTCTACCCCGAGCGCCTGGCGGGCCGCATCCTGGGCATGGGGGACGTGGCCAGCCTG GCGGAGAAGGTGCGGGCGGCGGGGCTGGAGGCGGAGGCGCCCAAGTCCGCCAAGGAGCTT TCCCTGGAGGACTTCCTCAAGCAGATGCAGAACCTCAAGCGCCTGGGCCCCTTCTCCGAG ATCCTGGGCCTCCTGCCCGGGGTTCCCCAGGGGCTTAAGGTGGACGAGAAGGCCATAAAG CGCCTGGAGGCCATCGTCCTCTCCATGACCCCCGAGGAGCGCAAAGACCCCCGCATCCTA AACGGTTCCCGGCGCAAGCGCATCGCCAAGGGAAGCGGGACCTCGGTCCAGGAGGTCAAC CGCTTCATCAAGGCATTTGAGGAGATGAAGGCCCTAATGAAGTCCCTGGAGAAGAAGAAG GGCCGGGGACTCATGGGAATGTTCAGGAGGTAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Freymann DM, Keenan RJ, Stroud RM, Walter P: Structure of the conserved GTPase domain of the signal recognition particle. Nature. 1997 Jan 23;385(6614):361-4. [9002524 ] Keenan RJ, Freymann DM, Walter P, Stroud RM: Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell. 1998 Jul 24;94(2):181-91. [9695947 ] Freymann DM, Keenan RJ, Stroud RM, Walter P: Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol. 1999 Aug;6(8):793-801. [10426959 ] Shepotinovskaya IV, Focia PJ, Freymann DM: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1834-7. Epub 2003 Sep 19. [14501130 ]

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