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 10-APR-2019, entry version 130. DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306}; DE Short=Ffh; DE AltName: Full=p48; GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; GN OrderedLocusNames=b2610, JW5414; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 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 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 277:1453-1462(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 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 FUNCTION, AND SUBUNIT. RX 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 FUNCTION, AND SUBUNIT. RX 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 FUNCTION, AND SUBUNIT. RX PubMed=9305630; DOI=10.1093/emboj/16.16.4880; RA Powers T., Walter P.; RT "Co-translational protein targeting catalyzed by the Escherichia coli RT signal recognition particle and its receptor."; RL EMBO J. 16:4880-4886(1997). RN [9] RP FUNCTION, GTPASE ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=11735405; DOI=10.1021/bi011639y; RA Peluso P., Shan S.O., Nock S., Herschlag D., Walter P.; RT "Role of SRP RNA in the GTPase cycles of Ffh and FtsY."; RL Biochemistry 40:15224-15233(2001). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=K12; RX PubMed=11741850; DOI=10.1128/JB.184.1.111-118.2002; RA Tian H., Beckwith J.; RT "Genetic screen yields mutations in genes encoding all known RT components of the Escherichia coli signal recognition particle RT pathway."; RL J. Bacteriol. 184:111-118(2002). RN [11] RP INTERACTION WITH RIBOSOMAL PROTEIN L23 AND 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 [12] RP INTERACTION WITH RIBOSOMAL PROTEIN L23, AND DOMAIN. 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 [13] 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 [14] 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 [15] RP REVIEW. RX PubMed=20682283; DOI=10.1016/j.bbamem.2010.07.025; RA Bibi E.; RT "Early targeting events during membrane protein biogenesis in RT Escherichia coli."; RL Biochim. Biophys. Acta 1808:841-850(2011). RN [16] RP STRUCTURE BY NMR OF 410-434. RX 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). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 371-430 IN COMPLEX WITH 4.5S RP RNA, AND DOMAIN. RX PubMed=10678824; DOI=10.1126/science.287.5456.1232; RA Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A.; RT "Crystal structure of the ribonucleoprotein core of the signal RT recognition particle."; RL Science 287:1232-1239(2000). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 328-432, AND SUBUNIT. RX PubMed=12269812; DOI=10.1021/bi026163c; RA Batey R.T., Doudna J.A.; RT "Structural and energetic analysis of metal ions essential to SRP RT signal recognition domain assembly."; RL Biochemistry 41:11703-11710(2002). RN [19] RP X-RAY CRYSTALLOGRAPHY (8.00 ANGSTROMS) OF 2-431. RX PubMed=17086193; DOI=10.1038/nature05326; RA Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., RA Sinning I., Beckmann R.; RT "Following the signal sequence from ribosomal tunnel exit to signal RT recognition particle."; RL Nature 444:507-511(2006). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 329-430. RX PubMed=17637337; DOI=10.1016/j.str.2007.06.003; RA Keel A.Y., Rambo R.P., Batey R.T., Kieft J.S.; RT "A general strategy to solve the phase problem in RNA RT crystallography."; RL Structure 15:761-772(2007). RN [21] RP X-RAY CRYSTALLOGRAPHY (13.50 ANGSTROMS) OF 371-430. RX PubMed=21151118; DOI=10.1038/nsmb.1952; RA Estrozi L.F., Boehringer D., Shan S.O., Ban N., Schaffitzel C.; RT "Cryo-EM structure of the E. coli translating ribosome in complex with RT SRP and its receptor."; RL Nat. Struct. Mol. Biol. 18:88-90(2011). RN [22] RP X-RAY CRYSTALLOGRAPHY (3.94 ANGSTROMS) OF 1-433. RX PubMed=21330537; DOI=10.1126/science.1196473; RA Ataide S.F., Schmitz N., Shen K., Ke A., Shan S.O., Doudna J.A., RA Ban N.; RT "The crystal structure of the signal recognition particle in complex RT with its receptor."; RL Science 331:881-886(2011). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic CC signal sequence of the ribosome-nascent chain (RNC) as it emerges CC from the ribosomes. The SRP-RNC complex is then targeted to the CC cytoplasmic membrane where it interacts with the SRP receptor CC FtsY. Interaction with FtsY leads to the transfer of the RNC CC complex to the Sec translocase for insertion into the membrane, CC the hydrolysis of GTP by both Ffh and FtsY, and the dissociation CC of the SRP-FtsY complex into the individual components. CC {ECO:0000255|HAMAP-Rule:MF_00306, ECO:0000269|PubMed:11735405, CC ECO:0000269|PubMed:11741850, ECO:0000269|PubMed:1279430, CC ECO:0000269|PubMed:1331806, ECO:0000269|PubMed:15140892, CC ECO:0000269|PubMed:2171778, ECO:0000269|PubMed:9305630}. CC -!- ACTIVITY REGULATION: Conformation of the Ffh-FtsY complex and CC regulation of its GTPase activity are modulated by the 4.5S RNA. CC Formation of the FfH-FtsY complex leads to a mutual stimulation of CC both GTPases. {ECO:0000269|PubMed:11735405}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. Metal CC ions are essential for the formation and stability of the SRP CC complex. Interacts with the ribosomes, via ribosomal protein L23. CC Interacts with FtsY. {ECO:0000255|HAMAP-Rule:MF_00306, CC ECO:0000269|PubMed:10678824, ECO:0000269|PubMed:12269812, CC ECO:0000269|PubMed:12702815, ECO:0000269|PubMed:12756233, CC ECO:0000269|PubMed:1279430, ECO:0000269|PubMed:1331806, CC ECO:0000269|PubMed:9305630}. CC -!- INTERACTION: CC P10121:ftsY; NbExp=10; IntAct=EBI-369938, EBI-549067; CC P0AGB3:rpoH; NbExp=4; IntAct=EBI-369938, EBI-555342; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=The SRP-RNC complex is CC targeted to the cytoplasmic membrane. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which CC is responsible for interactions with the ribosome, the central G CC domain, which binds GTP, and the C-terminal M domain, which binds CC the RNA and the signal sequence of the RNC. {ECO:0000255|HAMAP- CC Rule:MF_00306, ECO:0000269|PubMed:10678824, CC ECO:0000269|PubMed:12702815}. 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 {ECO:0000269|PubMed:11741850, ECO:0000269|PubMed:15140892}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA25957.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; 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_000913.3. DR RefSeq; WP_000460035.1; NZ_LN832404.1. 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=329-428. DR PDB; 4C7O; X-ray; 2.60 A; A/C=1-298. DR PDB; 5AKA; EM; 5.70 A; 5=328-436. DR PDB; 5GAD; EM; 3.70 A; i=4-434. DR PDB; 5GAF; EM; 4.30 A; i=1-434. DR PDB; 5GAG; EM; 3.80 A; i=4-434. DR PDB; 5GAH; EM; 3.80 A; i=1-434. DR PDB; 5NCO; EM; 4.80 A; i=4-434. 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 PDBsum; 4C7O; -. DR PDBsum; 5AKA; -. DR PDBsum; 5GAD; -. DR PDBsum; 5GAF; -. DR PDBsum; 5GAG; -. DR PDBsum; 5GAH; -. DR PDBsum; 5NCO; -. DR ProteinModelPortal; P0AGD7; -. DR SMR; P0AGD7; -. DR BioGrid; 4262086; 316. DR DIP; DIP-31865N; -. DR IntAct; P0AGD7; 22. DR STRING; 511145.b2610; -. DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family. DR EPD; P0AGD7; -. DR jPOST; P0AGD7; -. DR PaxDb; P0AGD7; -. DR PRIDE; P0AGD7; -. DR EnsemblBacteria; AAC75659; AAC75659; b2610. DR EnsemblBacteria; BAA16495; BAA16495; BAA16495. DR GeneID; 947102; -. DR KEGG; ecj:JW5414; -. DR KEGG; eco:b2610; -. DR PATRIC; fig|1411691.4.peg.4129; -. DR EchoBASE; EB0296; -. DR EcoGene; EG10300; ffh. DR eggNOG; ENOG4105CB9; Bacteria. DR eggNOG; COG0541; LUCA. DR HOGENOM; HOG000036164; -. DR InParanoid; P0AGD7; -. DR KO; K03106; -. DR PhylomeDB; P0AGD7; -. DR BioCyc; EcoCyc:EG10300-MONOMER; -. DR BioCyc; ECOL316407:JW5414-MONOMER; -. DR EvolutionaryTrace; P0AGD7; -. DR PRO; PR:P0AGD7; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:EcoliWiki. DR GO; GO:0048500; C:signal recognition particle; IMP:EcoliWiki. 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:0006612; P:protein targeting to membrane; IMP:EcoliWiki. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.10.260.30; -; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR004780; SRP_Ffh. DR PANTHER; PTHR11564; PTHR11564; 1. DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 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; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Ribonucleoprotein; KW RNA-binding; Signal recognition particle. FT CHAIN 1 453 Signal recognition particle protein. FT /FTId=PRO_0000101153. FT NP_BIND 107 114 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 190 194 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 248 251 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT HELIX 5 15 {ECO:0000244|PDB:4C7O}. FT HELIX 24 40 {ECO:0000244|PDB:4C7O}. FT HELIX 45 60 {ECO:0000244|PDB:4C7O}. FT HELIX 70 86 {ECO:0000244|PDB:4C7O}. FT STRAND 96 106 {ECO:0000244|PDB:4C7O}. FT HELIX 113 126 {ECO:0000244|PDB:4C7O}. FT STRAND 132 136 {ECO:0000244|PDB:4C7O}. FT HELIX 144 155 {ECO:0000244|PDB:4C7O}. FT STRAND 158 160 {ECO:0000244|PDB:4C7O}. FT HELIX 168 181 {ECO:0000244|PDB:4C7O}. FT STRAND 185 190 {ECO:0000244|PDB:4C7O}. FT HELIX 199 212 {ECO:0000244|PDB:4C7O}. FT STRAND 215 222 {ECO:0000244|PDB:4C7O}. FT HELIX 229 239 {ECO:0000244|PDB:4C7O}. FT STRAND 244 248 {ECO:0000244|PDB:4C7O}. FT HELIX 258 266 {ECO:0000244|PDB:4C7O}. FT STRAND 270 274 {ECO:0000244|PDB:4C7O}. FT STRAND 276 278 {ECO:0000244|PDB:4C7O}. FT STRAND 282 284 {ECO:0000244|PDB:4C7O}. FT HELIX 287 295 {ECO:0000244|PDB:4C7O}. FT HELIX 331 338 {ECO:0000244|PDB:1HQ1}. FT HELIX 373 381 {ECO:0000244|PDB:1HQ1}. FT HELIX 385 389 {ECO:0000244|PDB:1HQ1}. FT HELIX 391 393 {ECO:0000244|PDB:1HQ1}. FT HELIX 396 405 {ECO:0000244|PDB:1HQ1}. FT HELIX 410 430 {ECO:0000244|PDB:1HQ1}. 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 //