ID A0A0F7FIH3_9CREN Unreviewed; 436 AA.
AC A0A0F7FIH3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|HAMAP-Rule:MF_00306};
DE Short=SRP54 {ECO:0000256|HAMAP-Rule:MF_00306};
DE EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00306};
GN Name=srp54 {ECO:0000256|HAMAP-Rule:MF_00306};
GN ORFNames=MA03_06825 {ECO:0000313|EMBL:AKG39010.1};
OS Infirmifilum uzonense.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Infirmifilum.
OX NCBI_TaxID=1550241 {ECO:0000313|EMBL:AKG39010.1, ECO:0000313|Proteomes:UP000067434};
RN [1] {ECO:0000313|EMBL:AKG39010.1, ECO:0000313|Proteomes:UP000067434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1807-2 {ECO:0000313|EMBL:AKG39010.1,
RC ECO:0000313|Proteomes:UP000067434};
RX PubMed=26664700; DOI=10.1186/s40793-015-0105-y;
RA Toshchakov S.V., Korzhenkov A.A., Samarov N.I., Mazunin I.O., Mozhey O.I.,
RA Shmyr I.S., Derbikova K.S., Taranov E.A., Dominova I.N.,
RA Bonch-Osmolovskaya E.A., Patrushev M.V., Podosokorskaya O.A.,
RA Kublanov I.V.;
RT "Complete genome sequence of and proposal of Thermofilum uzonense sp. nov.
RT a novel hyperthermophilic crenarchaeon and emended description of the genus
RT Thermofilum.";
RL Stand. Genomic Sci. 10:122-122(2015).
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:0000256|HAMAP-Rule:MF_00306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}.
CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC {ECO:0000256|HAMAP-Rule:MF_00306}.
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:0000256|HAMAP-Rule:MF_00306}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|HAMAP-Rule:MF_00306}.
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DR EMBL; CP009961; AKG39010.1; -; Genomic_DNA.
DR RefSeq; WP_052884537.1; NZ_CP009961.1.
DR AlphaFoldDB; A0A0F7FIH3; -.
DR STRING; 1550241.MA03_06825; -.
DR GeneID; 25401930; -.
DR KEGG; thf:MA03_06825; -.
DR PATRIC; fig|1550241.5.peg.1415; -.
DR HOGENOM; CLU_009301_6_0_2; -.
DR OrthoDB; 52849at2157; -.
DR Proteomes; UP000067434; 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:0016887; F:ATP hydrolysis activity; 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 CDD; cd17875; SRP54_G; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 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:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 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; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00306};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00306};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00306};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00306}; Reference proteome {ECO:0000313|Proteomes:UP000067434};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00306};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00306};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW ECO:0000256|HAMAP-Rule:MF_00306}.
FT DOMAIN 1..85
FT /note="Signal recognition particle SRP54 helical bundle"
FT /evidence="ECO:0000259|SMART:SM00963"
FT DOMAIN 98..249
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 99..294
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|SMART:SM00962"
FT BINDING 106..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 188..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 246..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 436 AA; 48632 MW; 653ABE6F6E414F19 CRC64;
MESLRASLLG VVEKIRNSVL LDTRDVDAII RDLQRVLLKA DVDVKLVFDL SERIKKRFFS
QEIPSGFSKR DVLIKILYEE LVTLLGGENT TPYVVPKTPY TIMLVGIEGS GKTTTAAKLA
KYFKEQGYRV GLIAADTYRP GAHDQLKQLA EKIGVYFYGN PHSKTPLAIV EEGVKELTSK
NVQILIIDTA GRHKDEEALM REVVEIHESL KPDDVMLIID ATLGKEVSRQ AAAFHERIPL
GHVIITKLDG SARGGGALSA VAATGARIAF IGTGEKLEDL EPFVPQKFVA RLLGMPDLEA
LIKRFQAVEA VERERAKLIA SGKITLLDLK EQLLEVRKLG PLSKVLEMLG GSSLPLKGSI
EGSEEEFDKW IAIMNSMTQE ELLKPEIIDR SRMMRIARGS GTSVRDVRKL LDSYHQMRKL
VRQLYRSRRR IPGLNL
//