ID A0A2I0P556_9EURY Unreviewed; 360 AA.
AC A0A2I0P556;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CVV31_11925 {ECO:0000313|EMBL:PKL61376.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-2.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013818 {ECO:0000313|EMBL:PKL61376.1, ECO:0000313|Proteomes:UP000233573};
RN [1] {ECO:0000313|EMBL:PKL61376.1, ECO:0000313|Proteomes:UP000233573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-2 {ECO:0000313|EMBL:PKL61376.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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}.
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:PKL61376.1}.
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DR EMBL; PGYL01000037; PKL61376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0P556; -.
DR Proteomes; UP000233573; 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}.
FT DOMAIN 330..343
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT BINDING 169..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 251..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 309..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 360 AA; 39348 MW; 965E21B8D1252B72 CRC64;
MFDSLKKKLQ TIRDKFTSNI EEAAGTEPVP PVVEVPEVAE PAPSRVLLPE PPVSEEVLEK
EREEPTFFNK IKVLVREREV LLQEKDIEEP LSELEMVLLE NDVALPVTDE IIARMRRDLV
GRHRKIGSSV DGLVVTTLRS ALCGVLGEGL DLREYIAGHE RPVKILFTGV NGTGKTTTVA
KVGHYLQKNG FSVVIGAGDT FRAGAIEQIR THADRLGIKV IQHQAGADPS AVLFDAVQYA
KAHEIDVVLA DTAGRFHNRA NLMNQLEKIR RVMKPDLVVY VDEAVAGNDA VIRADEFNKA
VGTDAVVLTK ADMDPRGGAA ISVAHTVGKP ILFLGIGQGY DDIMPFEPRA MVNELLGDEA
//