ID A0A087ANZ9_9BIFI Unreviewed; 549 AA.
AC A0A087ANZ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:HJG40833.1};
GN ORFNames=BIGA_1092 {ECO:0000313|EMBL:KFI60499.1}, K8U73_00280
GN {ECO:0000313|EMBL:HJG40833.1};
OS Bifidobacterium pullorum subsp. gallinarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI60499.1, ECO:0000313|Proteomes:UP000029046};
RN [1] {ECO:0000313|EMBL:KFI60499.1, ECO:0000313|Proteomes:UP000029046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI60499.1,
RC ECO:0000313|Proteomes:UP000029046};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HJG40833.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ChiBcolR7-4860 {ECO:0000313|EMBL:HJG40833.1};
RX PubMed=33868800;
RA Gilroy R., Ravi A., Getino M., Pursley I., Horton D.L., Alikhan N.F.,
RA Baker D., Gharbi K., Hall N., Watson M., Adriaenssens E.M.,
RA Foster-Nyarko E., Jarju S., Secka A., Antonio M., Oren A., Chaudhuri R.R.,
RA La Ragione R., Hildebrand F., Pallen M.J.;
RT "Extensive microbial diversity within the chicken gut microbiome revealed
RT by metagenomics and culture.";
RL PeerJ 9:0-0(2021).
RN [3] {ECO:0000313|EMBL:HJG40833.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ChiBcolR7-4860 {ECO:0000313|EMBL:HJG40833.1};
RA Gilroy R.;
RL Submitted (SEP-2021) 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 + 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|ARBA:ARBA00035577, 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:KFI60499.1}.
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DR EMBL; DYUX01000001; HJG40833.1; -; Genomic_DNA.
DR EMBL; JGYX01000005; KFI60499.1; -; Genomic_DNA.
DR RefSeq; WP_033505397.1; NZ_JGYX01000005.1.
DR AlphaFoldDB; A0A087ANZ9; -.
DR eggNOG; COG0541; Bacteria.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000029046; Unassembled WGS sequence.
DR Proteomes; UP000786560; 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 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: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; 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:UP000029046};
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 287..300
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 163..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 208..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 266..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 549 AA; 58410 MW; 6055AC7E2F1E04BD CRC64;
MAAFSSLTDR LSNAFKHLKS KGKLSEADID GTIREIRRAL LDADVALEVV RSFTGRIRER
ALGTEVSEAL NPAQQVVKIV YDELTGVLGQ GVDRPLNFAK NPPTIIMLAG LQGAGKTTLA
GKLGYWLKDA GHTPLLVAAD LQRPNAVTQL QVVGERAGVP VYAPEKGVQS DGGDEVSAPG
LTTGDPVKVA RDSIALAKQK LYDTVIIDTA GRLGVDEVLM QQARDIRDAV QPDEILFVID
AMIGQDAVRT AKAFDEGVDF TGVVLSKLDG DARGGAALSV ASVTGKPILF ASTGEGLKDF
EVFHPDRMAS RILDMGDILT LIEQAQKQFD EEEARKAAQK MAEGEFGLDD FLEQLQQVRK
LGSMKSLLGM IPGMAQHRQA LEQFDEREID RTEAIIRSMT PAERRNPKII DGSRRARIAY
GSGVTVSQVN ALLQRFEQAA KMMKRMSNKA GMGGIPGFGG PAAGGKKGKK GKKKGSKSGN
PMKREAEEKA LRDRLSGKGG SSGSSGGSAF AKKPQNPALP AGLQDMLGEN GMPDVPPNLG
GGLGGLFGR
//
