ID A0A2Z4LBG1_9EURY Unreviewed; 459 AA.
AC A0A2Z4LBG1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AW729_04405 {ECO:0000313|EMBL:AWX33597.1};
OS Methanosphaera sp. BMS.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1789762 {ECO:0000313|EMBL:AWX33597.1, ECO:0000313|Proteomes:UP000249370};
RN [1] {ECO:0000313|Proteomes:UP000249370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMS {ECO:0000313|Proteomes:UP000249370};
RA O Cuiv P.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AWX33597.1, ECO:0000313|Proteomes:UP000249370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMS {ECO:0000313|EMBL:AWX33597.1,
RC ECO:0000313|Proteomes:UP000249370};
RA Morrison M.;
RT "Methanosphaera spp. pan-genomic study of isolate and population genomes.";
RL Submitted (JUN-2018) 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|HAMAP-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}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00920}.
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DR EMBL; CP014213; AWX33597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4LBG1; -.
DR KEGG; metb:AW729_04405; -.
DR Proteomes; UP000249370; 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: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}.
FT DOMAIN 431..444
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 352..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 410..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 459 AA; 51967 MW; F1C27339C3020AE8 CRC64;
MDKEDEESGP EDTDEDTQEE GEKDTDKKDS EKSDTVDKQK TEETKKGRFS FFRRNKKEEE
KPEESDEEDE KVEEDIAQDE EDTSEDTSDD VTEETSSTNE STEETKEEEK KEEKKGRFSF
FRRNKKEEEK TEEAKTEEKT ETTEETTQDE EDKKEPAKQA KKDEEESGGM FSFITKKTIK
EDDISDILDE LFMSLLEGDV AYEVADRIVE SVKEDLIGKK IQRRGDMELF TTNALKKAIT
EIIDNGSFDL LGEIEKSKQN GEPYKIMFVG INGTGKTTTI AKMATYLEKH GYSSVFGASD
TFRAGAIEQL EHHAKKLNLK IIKHERNSDP AAVAYDAVEH AKATGKNVVL IDTSGRMQTN
ANLMDEMKKI KRVSQPDFVM YVGDALMGND ATEQATKFNE VIDIDGIILT KADADAKGGA
ALSIGHVIHK PILFIGTGQS YDDLMEFKPE WMINLIFEE
//
