SRP54_HALVD
ID SRP54_HALVD Reviewed; 465 AA.
AC Q977V2; D4GYW9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE Short=SRP54 {ECO:0000255|HAMAP-Rule:MF_00306};
DE AltName: Full=Hv54h;
GN Name=srp54 {ECO:0000255|HAMAP-Rule:MF_00306}; Synonyms=hv54h;
GN OrderedLocusNames=HVO_0123;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH SRP19 AND 7S RNA,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DSM 5716 / WFD11;
RX PubMed=12029042; DOI=10.1128/jb.184.12.3260-3267.2002;
RA Rose R.W., Pohlschroder M.;
RT "In vivo analysis of an essential archaeal signal recognition particle in
RT its native host.";
RL J. Bacteriol. 184:3260-3267(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=12364595; DOI=10.1093/nar/gkf548;
RA Tozik I., Huang Q., Zwieb C., Eichler J.;
RT "Reconstitution of the signal recognition particle of the halophilic
RT archaeon Haloferax volcanii.";
RL Nucleic Acids Res. 30:4166-4175(2002).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. Archaeal SRP consists of a
CC 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and
CC SRP19. {ECO:0000255|HAMAP-Rule:MF_00306, ECO:0000269|PubMed:12364595}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306,
CC ECO:0000269|PubMed:12029042, ECO:0000269|PubMed:12364595}. Note=The
CC SRP-RNC complex is targeted to 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 -!- DISRUPTION PHENOTYPE: Cannot be disrupted, it is thus essential.
CC {ECO:0000269|PubMed:12029042}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; AF395887; AAK93963.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03670.1; -; Genomic_DNA.
DR RefSeq; WP_004045235.1; NZ_AOHU01000105.1.
DR AlphaFoldDB; Q977V2; -.
DR SMR; Q977V2; -.
DR STRING; 309800.C498_18853; -.
DR EnsemblBacteria; ADE03670; ADE03670; HVO_0123.
DR GeneID; 8925329; -.
DR KEGG; hvo:HVO_0123; -.
DR eggNOG; arCOG01228; Archaea.
DR HOGENOM; CLU_009301_6_0_2; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 25871at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule.
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; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 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; SSF47364; SSF47364; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..465
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101175"
FT BINDING 104..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 184..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 242..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ SEQUENCE 465 AA; 50918 MW; 9F5705838DFF8370 CRC64;
MVLDNLGSSL RGSLDKLRGK SRLDEDDVQE IVKEIQRSLL SADVDVSLVM DLSDSIKTRA
LEEEPPGGTS ARDHVLKIVY EELVDLIGES TEIPLESQTI MLAGLQGSGK TTTSAKMAWW
FSKKGLRPAV IQTDTFRPGA YDQAKQMCER AEVDFYGDPD CDDPVQIARE GLEATEDADV
HIVDTAGRHA LEDDLIDEIE EIEGVVQPDL NLLVLDAAIG QGAKEQAQQF DESIGIGGVV
ITKLDGTAKG GGALTAVNET DSSIAFLGMG ETVQDIERFE PNGFISRLLG MGDLKQLSER
VERAMSETQA EDEDWDPEEM MKGNFTLKDM QKQMEAMDKM GPLDQVLDMI PGFGGGIKDQ
LPDDAMDVTK DRMRSFEVIM DSMTEEELEN PRKVGASRVR RIAQGSGQDE ETIQELLEQH
RMMEQTIKQF QNMGDGDMQR MMKKLQNQGG GGGGGMGGLG GMGPF
