ID A0A1B1AT60_9ACTN Unreviewed; 403 AA.
AC A0A1B1AT60;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AVL59_09050 {ECO:0000313|EMBL:ANP49735.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP49735.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP49735.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP49735.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016279; ANP49735.1; -; Genomic_DNA.
DR RefSeq; WP_067301315.1; NZ_JAGGLP010000009.1.
DR AlphaFoldDB; A0A1B1AT60; -.
DR STRING; 68214.AVL59_09050; -.
DR KEGG; sgs:AVL59_09050; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000092659; 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 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; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43134:SF1; 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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00920}; 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}.
FT DOMAIN 375..388
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 25..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 292..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 354..357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 403 AA; 42693 MW; D6050DE88C0F3463 CRC64;
METVILAVVI AVVVLAALGG LVVGSRRRKP LPPPPPTTPD ITAPPAEPHV GDEAETPRDE
PRRTIEEVDL PGGSAPVAVE EPPAVPAVEA PEIEIPEPTA GRLIRLRARL SRSQNALGKG
LLTLLSREHL DEDTWEEIED TLLTADVGVQ PTQELVERLR ERVKVLGTRT PGELRDLLRE
ELLKLVGTDV DRAVKTEPED RRPGIVMVVG VNGTGKTTTT GKLGRVLVAD GRTVVLGAAD
TFRAAAADQL QTWGERVGAY TVRGPEGGDP ASVAFDAVKE GKEMGVDVVL IDTAGRLHTK
TGLMDELGKV KRVVEKHAPL DEVLLVLDAT TGQNGLVQAR VFAEVVDITG IVLTKLDGTA
KGGIVVAVQR ELGVPVKLIG LGEGADDLAP FEPEAFVDAL IGD
//