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 16-MAY-2012, entry version 69. DE RecName: Full=Signal recognition particle protein; DE AltName: Full=Fifty-four homolog; DE Short=Ffh; DE AltName: Full=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 FUNCTION IN LIPOPROTEIN EXPORT, AND DISRUPTION PHENOTYPE. RX PubMed=15140892; DOI=10.1074/jbc.M403229200; RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.; RT "Targeting and translocation of two lipoproteins in Escherichia coli RT via the SRP/Sec/YidC pathway."; RL J. Biol. Chem. 279:31026-31032(2004). RN [11] 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 [12] 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, including at least some lipoproteins. Binds to the CC signal sequence when it emerges from the ribosomes. This binding CC is mediated at least in part by ribosomal protein L23 CC (PubMed:12756233, PubMed:12702815 and 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 -!- DISRUPTION PHENOTYPE: Essential; deletion experiments lead to loss CC of inner membrane protein targeting. Also leads to reduced CC targeting of lipoproteins Lpp and BRP. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA25957.1; Type=Erroneous initiation; Note=Translation N-terminally extended; 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; NP_417101.1; NC_000913.2. DR PDB; 1DUL; X-ray; 1.80 A; A=371-430. DR PDB; 1HQ1; X-ray; 1.52 A; A=328-432. DR PDB; 2J28; EM; 8.00 A; 9=2-431. DR PDB; 2PXB; X-ray; 2.00 A; A=329-430. DR PDB; 2PXD; X-ray; 2.00 A; A=329-430. DR PDB; 2PXE; X-ray; 2.00 A; A=329-430. DR PDB; 2PXF; X-ray; 2.00 A; A=329-430. DR PDB; 2PXK; X-ray; 2.00 A; A=329-430. DR PDB; 2PXL; X-ray; 2.50 A; A=329-430. DR PDB; 2PXP; X-ray; 2.50 A; A=329-430. DR PDB; 2PXQ; X-ray; 2.50 A; A=329-430. DR PDB; 2PXT; X-ray; 2.50 A; A=329-430. DR PDB; 2PXU; X-ray; 2.50 A; A=329-430. DR PDB; 2PXV; X-ray; 2.00 A; A=329-430. DR PDB; 2XKV; EM; 13.50 A; C=371-430. DR PDB; 2XXA; X-ray; 3.94 A; A/C=1-433. DR PDB; 3LQX; X-ray; 1.93 A; A=328-432. DR PDBsum; 1DUL; -. DR PDBsum; 1HQ1; -. DR PDBsum; 2J28; -. DR PDBsum; 2PXB; -. DR PDBsum; 2PXD; -. DR PDBsum; 2PXE; -. DR PDBsum; 2PXF; -. DR PDBsum; 2PXK; -. DR PDBsum; 2PXL; -. DR PDBsum; 2PXP; -. DR PDBsum; 2PXQ; -. DR PDBsum; 2PXT; -. DR PDBsum; 2PXU; -. DR PDBsum; 2PXV; -. DR PDBsum; 2XKV; -. DR PDBsum; 2XXA; -. DR PDBsum; 3LQX; -. DR ProteinModelPortal; P0AGD7; -. DR SMR; P0AGD7; 2-431. DR DIP; DIP-31865N; -. DR IntAct; P0AGD7; 17. DR MINT; MINT-1218614; -. DR TCDB; 3.A.5.1.1; general secretory pathway (Sec) family. DR EnsemblBacteria; EBESCT00000004690; EBESCP00000004690; EBESCG00000003831. DR EnsemblBacteria; EBESCT00000014850; EBESCP00000014141; EBESCG00000013910. DR GeneID; 947102; -. DR GenomeReviews; AP009048_GR; JW5414. DR GenomeReviews; U00096_GR; b2610. DR KEGG; eco:b2610; -. DR PATRIC; 32120619; VBIEscCol129921_2708. DR EchoBASE; EB0296; -. DR EcoGene; EG10300; ffh. DR eggNOG; COG0541; -. DR HOGENOM; HOG000036164; -. DR KO; K03106; -. DR OMA; IINGSRR; -. DR ProtClustDB; PRK10867; -. DR BioCyc; EcoCyc:EG10300-MONOMER; -. DR EvolutionaryTrace; P0AGD7; -. DR Genevestigator; P0AGD7; -. DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW. DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IDA:EcoliWiki. DR GO; GO:0003924; F:GTPase activity; IMP:EcoCyc. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; G3DSA:1.20.120.140; SRP54_helical; 1. DR Gene3D; G3DSA:1.10.260.30; SRP54_M; 1. DR InterPro; IPR003593; AAA+_ATPase. 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 PANTHER; PTHR11564:SF7; SRP_sub; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47446; Signal_recog_particle_SRP54_M; 1. DR SUPFAM; SSF47364; SRP54; 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 Reference proteome; Ribonucleoprotein; RNA-binding; KW 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 HELIX 331 336 FT HELIX 372 381 FT HELIX 385 389 FT HELIX 391 393 FT HELIX 396 405 FT HELIX 410 429 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 //