ID SRP54_ECOLI Reviewed; 453 AA. AC P0AGD7; P07019; P77007; P77008; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 23-OCT-2007, entry version 24. DE Signal recognition particle protein (Fifty-four homolog) (p48). GN Name=ffh; OrderedLocusNames=b2610, JW5414; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84057772; PubMed=6357787; RA Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.; RT "The nucleotide sequence of an Escherichia coli operon containing RT genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 RT and L19 and a 21-K polypeptide."; RL EMBO J. 2:899-905(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP FUNCTION. RX MEDLINE=91029490; PubMed=2171778; DOI=10.1016/0092-8674(90)90454-M; RA Ribes V., Roemisch K., Giner A., Dobberstein B., Tollervey D.; RT "E. coli 4.5S RNA is part of a ribonucleoprotein particle that has RT properties related to signal recognition particle."; RL Cell 63:591-600(1990). RN [6] RP CHARACTERIZATION. RX MEDLINE=93063265; PubMed=1279430; DOI=10.1038/359741a0; RA Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B.; RT "Signal-sequence recognition by an Escherichia coli ribonucleoprotein RT complex."; RL Nature 359:741-743(1992). RN [7] RP CHARACTERIZATION. RX MEDLINE=93063266; PubMed=1331806; DOI=10.1038/359744a0; RA Phillips G.J., Silhavy T.J.; RT "The E. coli ffh gene is necessary for viability and efficient protein RT export."; RL Nature 359:744-746(1992). RN [8] RP CROSS-LINKS TO RIBOSOMAL PROTEIN L23 AND TO NASCENT PROTEIN CHAINS. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=12756233; DOI=10.1083/jcb.200302130; RA Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., RA Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.; RT "Interplay of signal recognition particle and trigger factor at L23 RT near the nascent chain exit site on the Escherichia coli ribosome."; RL J. Cell Biol. 161:679-684(2003). RN [9] RP IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RP RECOGNITION PARTICLE. RC STRAIN=MRE-600; RX PubMed=12702815; DOI=10.1261/rna.2196403; RA Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.; RT "The signal recognition particle binds to protein L23 at the peptide RT exit of the Escherichia coli ribosome."; RL RNA 9:566-573(2003). RN [10] RP SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME. RC STRAIN=MRE-600; RX PubMed=15148364; DOI=10.1073/pnas.0402231101; RA Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., RA Bukau B., Wintermeyer W.; RT "Trigger factor binds to ribosome-signal-recognition particle (SRP) RT complexes and is excluded by binding of the SRP receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004). RN [11] RP STRUCTURE BY NMR OF 410-434. RX MEDLINE=97053672; PubMed=8898086; DOI=10.1016/0014-5793(96)01019-8; RA Oh D.-B., Yi G.-S., Chi S.-W., Kim H.; RT "Structure of a methionine-rich segment of Escherichia coli Ffh RT protein."; RL FEBS Lett. 395:160-164(1996). CC -!- FUNCTION: Necessary for efficient export of extracytoplasmic CC proteins. Binds to the signal sequence when it emerges from the CC ribosomes. This binding is mediated at least in part by ribosomal CC protein L23 (PubMed:12756233, PubMed:12702815 and CC PubMed:15148364). CC -!- SUBUNIT: Signal recognition particle consists of a 4.5 RNA CC molecule and protein ffh. CC -!- DOMAIN: The protein has a two domain structure: the G-domain binds CC GTP; the M-domain binds the RNA and also binds the signal CC sequence. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X01818; CAA25957.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC75659.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16495.2; -; Genomic_DNA. DR PIR; E65039; E65039. DR RefSeq; AP_003191.1; -. DR RefSeq; NP_417101.1; -. DR PDB; 1DUL; X-ray; A=371-430. DR PDB; 1HQ1; X-ray; A=328-432. DR IntAct; P0AGD7; -. DR GeneID; 947102; -. DR GenomeReviews; U00096_GR; b2610. DR GenomeReviews; AP009048_GR; JW5414. DR KEGG; ecj:JW5414; -. DR KEGG; eco:b2610; -. DR EchoBASE; EB0296; -. DR EcoGene; EG10300; ffh. DR BioCyc; EcoCyc:EG10300-MONOMER; -. DR InterPro; IPR003593; AAA+_ATPase_core. DR InterPro; IPR000897; Signal_recog_part_SRP54_GTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004780; Signal_recog_particle_SRP. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR Gene3D; G3DSA:1.20.120.140; SRP54_helical; 1. DR Gene3D; G3DSA:1.10.260.30; SRP54_M; 1. DR PANTHER; PTHR11564:SF7; SRP_sub; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR ProDom; PD000819; SRP54; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; GTP-binding; Nucleotide-binding; KW Ribonucleoprotein; RNA-binding; Signal recognition particle. FT CHAIN 1 453 Signal recognition particle protein. FT /FTId=PRO_0000101153. FT NP_BIND 107 114 GTP (By similarity). FT NP_BIND 190 194 GTP (By similarity). FT NP_BIND 248 251 GTP (By similarity). FT REGION 1 295 G-domain. FT REGION 296 453 M-domain. FT TURN 3 7 FT HELIX 8 12 FT HELIX 26 39 FT HELIX 46 59 FT STRAND 66 68 FT HELIX 70 85 FT STRAND 97 100 FT STRAND 102 106 FT STRAND 108 113 FT TURN 114 116 FT HELIX 117 125 FT STRAND 127 129 FT STRAND 140 142 FT HELIX 145 154 FT HELIX 170 181 FT STRAND 187 191 FT HELIX 198 209 FT STRAND 215 222 FT TURN 223 225 FT HELIX 226 229 FT HELIX 230 237 FT STRAND 244 248 FT STRAND 250 252 FT HELIX 258 264 FT TURN 265 267 FT STRAND 276 278 FT HELIX 287 289 FT HELIX 302 310 FT TURN 311 313 FT STRAND 319 323 FT HELIX 335 339 FT TURN 342 345 FT TURN 365 368 FT STRAND 374 377 FT TURN 378 382 FT HELIX 386 389 FT TURN 397 399 FT HELIX 400 405 FT HELIX 410 412 FT HELIX 414 427 SQ SEQUENCE 453 AA; 49787 MW; E9C7A7101CC04D66 CRC64; MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE FINRVKEKAV GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP AVVLMAGLQG AGKTTSVGKL GKFLREKHKK KVLVVSADVY RPAAIKQLET LAEQVGVDFF PSDVGQKPVD IVNAALKEAK LKFYDVLLVD TAGRLHVDEA MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL PLTGVVLTKV DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL MGKLPGMGQI PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR RIAAGCGMQV QDVNRLLKQF DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF PGR //