ID A0A2G1XCQ6_STRCJ Unreviewed; 413 AA.
AC A0A2G1XCQ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=BLA24_23370 {ECO:0000313|EMBL:PHQ49037.1}, CYQ11_22705
GN {ECO:0000313|EMBL:PPT15317.1};
OS Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ49037.1, ECO:0000313|Proteomes:UP000222531};
RN [1] {ECO:0000313|EMBL:PHQ49037.1, ECO:0000313|Proteomes:UP000222531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ49037.1,
RC ECO:0000313|Proteomes:UP000222531};
RX PubMed=29053243;
RA Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT "Identification of the Biosynthetic Pathway for the Antibiotic
RT Bicyclomycin.";
RL Biochemistry 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:PPT15317.1, ECO:0000313|Proteomes:UP000239771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT15317.1,
RC ECO:0000313|Proteomes:UP000239771};
RA Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT bacterial classes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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). {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. {ECO:0000256|HAMAP-
CC Rule:MF_00920}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00920};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}. Cytoplasm
CC {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}.
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:PHQ49037.1}.
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DR EMBL; NHZO01000154; PHQ49037.1; -; Genomic_DNA.
DR EMBL; PKFQ01000001; PPT15317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1XCQ6; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000222531; Unassembled WGS sequence.
DR Proteomes; UP000239771; Unassembled WGS sequence.
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 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; IPR036225; SRP/SRP_N.
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; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
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:UP000222531}.
FT DOMAIN 385..398
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 25..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 302..306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 364..367
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 413 AA; 43268 MW; 886693399DA1D603 CRC64;
MEIVILAVVI AVVALGAISG LVVSSRKKKQ LPPAPPSSPS VTAPPAEPHV GEEAETPRAE
PRRTVEEVEL PEAPAEAETA PVVEPEAAAP AAPAEPEIEV PEPTAGRLVR LRARLSRSQN
SLGKGLLTLL SREHLDEDTW EEIEDTLLTA DVGVAPTQEL VERLRERVKV LGTRTPDELR
GLLREELLAL IGTDFDRSVH TEPGIGVNGE EKPGVVMVVG VNGTGKTTTT GKLARVLVAD
GKSVVLGAAD TFRAAAADQL QTWGERVGAR TVRGPEGGDP ASIAFDAVKE GIAEKADVVL
VDTAGRLHTK TGLMDELGKV KRVVEKHGSV DEVLLVLDAT TGQNGLVQAR VFAEVVDITG
IVLTKLDGTA KGGIVVAVQR ELGVPVKLVG LGEGADDLAP FEPEAFVDAL IGD
//
