ID A0A926T023_9CYAN Unreviewed; 486 AA.
AC A0A926T023;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 11.
DE RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306};
DE EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00306};
DE AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306};
GN Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306,
GN ECO:0000313|EMBL:MBD1923596.1};
GN ORFNames=H6F77_21335 {ECO:0000313|EMBL:MBD1923596.1};
OS Microcoleus sp. FACHB-831.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Microcoleus.
OX NCBI_TaxID=2692827 {ECO:0000313|EMBL:MBD1923596.1, ECO:0000313|Proteomes:UP000619409};
RN [1] {ECO:0000313|EMBL:MBD1923596.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-831 {ECO:0000313|EMBL:MBD1923596.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD1923596.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-831 {ECO:0000313|EMBL:MBD1923596.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 + phosphate + H(+); 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|ARBA:ARBA00048027, ECO:0000256|HAMAP-
CC Rule:MF_00306};
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. {ECO:0000256|HAMAP-
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBD1923596.1}.
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DR EMBL; JACJON010000068; MBD1923596.1; -; Genomic_DNA.
DR RefSeq; WP_190490972.1; NZ_JACJON010000068.1.
DR Proteomes; UP000619409; Unassembled WGS sequence.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
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; cd18539; SRP_G; 1.
DR FunFam; 3.40.50.300:FF:000022; Signal recognition particle 54 kDa subunit; 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; IPR004780; SRP.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR NCBIfam; TIGR00959; ffh; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE SUBUNIT 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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:UP000619409};
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 268..281
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 380..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 486 AA; 52693 MW; 2DDAA23153DE345D CRC64;
MFDALAERLE GAWKKLRGQD KISKSNIEDA LREVRRALLE ADVNLQVVKD FITGVETRAL
GADVVSGVRP DQQFIKIVYD ELVAVMGETN VPLAQADNSP TIVLMAGLQG TGKTTATAKL
ALHLRKQNIS TLLVATDIYR PAAIDQLLTL GQQIEVPVFQ LGTDADPVEI ARQGVAQAKA
TGVDMVIIDT AGRLQIDRDM MGELARIKET VQPHETLLVV DAMTGQEAAN LTRTFHQEIG
ITGAILTKLD GDTRGGAALS VRQISGQPIK FVGVGEKVEA LQPFYPDRMA SRILGMGDVL
TLVEKAQEEI DLADAQKMEE KILSAKFDFS DFLKQMRLLK NMGSLGGLMK LIPGMGKLSD
DQLRQGEIGL KRTEAMINSM TSEERKNPDL LSSTPSRRRR IARGSGYQES DVAKLVTDFK
KMRSLMQQMG QGGMPGMPGM PGMPGMFGGM GGGNMPARPG FRGYPGGVGA KKQQKKAKKK
KGFGQL
//
