SRP54_BACSU
ID SRP54_BACSU Reviewed; 446 AA.
AC P37105;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
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};
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=BSU15980;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8335643; DOI=10.1128/jb.175.15.4885-4894.1993;
RA Honda K., Nakamura K., Nishiguchi M., Yamane K.;
RT "Cloning and characterization of a Bacillus subtilis gene encoding a
RT homolog of the 54-kilodalton subunit of mammalian signal recognition
RT particle and Escherichia coli Ffh.";
RL J. Bacteriol. 175:4885-4894(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, GTPASE ACTIVITY, INTERACTION WITH RNA, AND SUBCELLULAR LOCATION.
RX PubMed=7511896; DOI=10.1006/bbrc.1994.1385;
RA Nakamura K., Nishiguchi M., Honda K., Yamane K.;
RT "The Bacillus subtilis SRP54 homologue, Ffh, has an intrinsic GTPase
RT activity and forms a ribonucleoprotein complex with small cytoplasmic RNA
RT in vivo.";
RL Biochem. Biophys. Res. Commun. 199:1394-1399(1994).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Binds to the hydrophobic signal
CC sequence of the ribosome-nascent chain (RNC) as it emerges from the
CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic
CC membrane where it interacts with the SRP receptor FtsY. Interaction
CC with FtsY leads to the transfer of the RNC complex to the Sec
CC translocase for insertion into the membrane, the hydrolysis of GTP by
CC both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into
CC the individual components (Probable). {ECO:0000305|PubMed:7511896}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY (By similarity). Interacts
CC with a small cytoplasmic RNA (sc-RNA). {ECO:0000255|HAMAP-
CC Rule:MF_00306, ECO:0000269|PubMed:7511896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306,
CC ECO:0000269|PubMed:7511896}. Note=The SRP-RNC complex is targeted to
CC the cytoplasmic membrane.
CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is
CC responsible for interactions with the ribosome, the central G domain,
CC which binds GTP, and the C-terminal M domain, which binds the RNA and
CC the signal sequence of the RNC. {ECO:0000255|HAMAP-Rule:MF_00306}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; D14356; BAA21691.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13471.1; -; Genomic_DNA.
DR PIR; B47154; B47154.
DR RefSeq; NP_389480.1; NC_000964.3.
DR RefSeq; WP_003232020.1; NZ_JNCM01000035.1.
DR PDB; 4UE4; EM; 7.00 A; C=330-431.
DR PDB; 7O5B; EM; 3.33 A; g=3-446.
DR PDB; 7O9F; X-ray; 2.51 A; A/B/C=3-300.
DR PDBsum; 4UE4; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7O9F; -.
DR AlphaFoldDB; P37105; -.
DR SMR; P37105; -.
DR IntAct; P37105; 1.
DR MINT; P37105; -.
DR STRING; 224308.BSU15980; -.
DR jPOST; P37105; -.
DR PaxDb; P37105; -.
DR PRIDE; P37105; -.
DR EnsemblBacteria; CAB13471; CAB13471; BSU_15980.
DR GeneID; 937104; -.
DR KEGG; bsu:BSU15980; -.
DR PATRIC; fig|224308.179.peg.1738; -.
DR eggNOG; COG0541; Bacteria.
DR InParanoid; P37105; -.
DR OMA; DTAGRHK; -.
DR PhylomeDB; P37105; -.
DR BioCyc; BSUB:BSU15980-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR004780; SRP.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
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; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..446
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101149"
FT BINDING 108..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ SEQUENCE 446 AA; 49541 MW; D71943B23374633D CRC64;
MAFEGLADRL QQTISKIRGK GKVSEQDVKE MMREVRLALL EADVNFKVVK DFVKKVSERA
VGQDVMKSLT PGQQVIKVVQ EELTELMGGE ESKIAVAKRP PTVIMMVGLQ GAGKTTTSGK
LANLLRKKHN RKPMLVAADI YRPAAIKQLE TLGKQLDMPV FSLGDQVSPV EIAKQAIEKA
KEEHYDYVIL DTAGRLHIDH ELMDELTNVK EIANPEEIFL VVDSMTGQDA VNVAKSFNEQ
LGLTGVVLTK LDGDTRGGAA LSIRAVTNTP IKFAGLGEKL DALEPFHPER MASRILGMGD
VLTLIEKAQA SVDEDKAKEL EQKMRTMSFT LDDFLEQLGQ VRNMGPLDEL LQMMPGAGKM
KGLKNIQVDE KQLNHVEAII KSMTVLEKEQ PDIINASRRK RIAKGSGTSV QEVNRLLKQF
DEMKKMMKQM TNMSKGKKKG FKLPFM
