ID G7URP0_PSEUP Unreviewed; 477 AA.
AC G7URP0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920};
DE EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920};
GN OrderedLocusNames=DSC_06335 {ECO:0000313|EMBL:AER55918.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55918.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER55918.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER55918.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Acts as a receptor for the
CC complex formed by the signal recognition particle (SRP) and the
CC ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the
CC transfer of the RNC complex to the Sec translocase for insertion into
CC the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the
CC dissociation of the SRP-FtsY complex into the individual components.
CC {ECO:0000256|HAMAP-Rule:MF_00920}.
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_00920};
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein
CC composed of Ffh and a 4.5S RNA molecule. {ECO:0000256|HAMAP-
CC Rule:MF_00920}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}.
CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00920}.
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DR EMBL; CP003093; AER55918.1; -; Genomic_DNA.
DR RefSeq; WP_014160095.1; NC_016147.2.
DR AlphaFoldDB; G7URP0; -.
DR STRING; 1045855.DSC_06335; -.
DR KEGG; psd:DSC_06335; -.
DR eggNOG; COG0552; Bacteria.
DR HOGENOM; CLU_009301_4_1_6; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd17874; FtsY; 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 HAMAP; MF_00920; FtsY; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004390; SR_rcpt_FtsY.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR NCBIfam; TIGR00064; ftsY; 1.
DR PANTHER; PTHR43134:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 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 PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00920}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00920};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00920};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|HAMAP-Rule:MF_00920};
KW Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT DOMAIN 444..457
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 359..363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 423..426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 477 AA; 49319 MW; 41C8444A248EC233 CRC64;
MVSFFRRKKP GDAPSGQDGN TRRYSVEELA AAFPEPRPAA PKQVDAAAAI EQARHGAPEQ
APATPPRTPD TQTFAPADGG QPEFVVPAPS PLRAEPAPLP VSPVAAEPAP APVAPAPAPA
EPVVPPTVAL APEVLPQPVA PTPAPAPAPT PTAEPIASGS LGTAERPAAP AGKAGWRERL
RGSVFARSFG GLFSRNPKLD EDLLDEIETA LITADVGVGA TTALVEALRK RMKAREFADA
NALLAALRAE LIAILRPVAV PLVIDPQAKP FVVLTVGVNG VGKTTTIGKL AKRFKDEGYS
LMLAAGDTFR AAAVAQLQAW GERNGVTVVA QGQNADAASV AFDALQAGKA RGTQVLIADT
AGRLHTQTGL MNELGKIRRV LGKLDPAAPH EVLMVIDGTT GQNALSQLRQ FHAAVGVTGL
VVTKLDGTAK GGVVFALARE FGIPIRYAGI GERPEDLRVF DAEAFVDALL PEALGSA
//
