FTSY_HALVD
ID FTSY_HALVD Reviewed; 456 AA.
AC D4GYW6; Q977F6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=HVO_0120;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-456, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=15030489; DOI=10.1111/j.1432-1033.2004.04050.x;
RA Lichi T., Ring G., Eichler J.;
RT "Membrane binding of SRP pathway components in the halophilic archaea
RT Haloferax volcanii.";
RL Eur. J. Biochem. 271:1382-1390(2004).
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:0000255|HAMAP-Rule:MF_00920}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. {ECO:0000255|HAMAP-
CC Rule:MF_00920}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00920,
CC ECO:0000269|PubMed:15030489}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00920, ECO:0000269|PubMed:15030489};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00920,
CC ECO:0000269|PubMed:15030489}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_00920, ECO:0000269|PubMed:15030489}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; CP001956; ADE05025.1; -; Genomic_DNA.
DR EMBL; AF439264; AAL30433.1; -; Genomic_DNA.
DR RefSeq; WP_004045232.1; NZ_AOHU01000105.1.
DR AlphaFoldDB; D4GYW6; -.
DR SMR; D4GYW6; -.
DR STRING; 309800.C498_18838; -.
DR EnsemblBacteria; ADE05025; ADE05025; HVO_0120.
DR GeneID; 8924270; -.
DR KEGG; hvo:HVO_0120; -.
DR eggNOG; arCOG01227; Archaea.
DR HOGENOM; CLU_009301_3_1_2; -.
DR OMA; GIEATDY; -.
DR OrthoDB; 90641at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
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; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00064; ftsY; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome.
FT CHAIN 1..456
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000416704"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 347..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 405..408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ SEQUENCE 456 AA; 48187 MW; 218AA04BA31279F2 CRC64;
MFDGLKKKLN RFRNDVEETA EEKAEAAADE AESDADAEAE SAPADTDNAA VEPEASEPAA
ADPDADAVGD ADAGSEADAV DAADAPADAE SSSAAVEADA ESESESAATP EPDSEVDAGA
DTGDEPSGEP TADEVEPRES LASDAAKAAL TEEDEDDSSG PGRLRRAAAF ATGKVVIEEE
DLEDPLWELE MALLQSDVEM QVAEEILETI REKLIGETRK QVESTGQLVS EALHDALYEV
ISVGQFDFDQ RIAEADKPVT LIFTGINGVG KTTTIAKLAK YFEKQGYSTV LANGDTYRAG
ANEQIREHAE ALDKKLIAHE QGGDPAAVIY DGVEYAEAHD IDIVLGDTAG RLHTSNDLMA
QLEKIDRVVG PDLTLFVDEA VAGQDAVERA RQFNDAAAID GAILTKADAD SNGGAAISIA
YVTGKPILFL GVGQGYDHIE KFDPEQMVER LLGEDE
