FTSY_SULAC
ID FTSY_SULAC Reviewed; 369 AA.
AC P27414; Q4J8U7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
DE AltName: Full=Docking protein;
DE AltName: Full=P41;
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; Synonyms=dpa, sso;
GN OrderedLocusNames=Saci_1462;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1658539; DOI=10.1111/j.1365-2958.1991.tb01916.x;
RA Ramirez C., Matheson A.T.;
RT "A gene in the archaebacterium Sulfolobus solfataricus that codes for a
RT protein equivalent to the alpha subunits of the signal recognition particle
RT receptor in eukaryotes.";
RL Mol. Microbiol. 5:1687-1693(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=8935656; DOI=10.1111/j.1574-6968.1996.tb08081.x;
RA Moll R., Schmidtke S., Schaefer G.;
RT "A putative signal recognition particle receptor alpha subunit (SR alpha)
RT homologue is expressed in the hyperthermophilic crenarchaeon Sulfolobus
RT acidocaldarius.";
RL FEMS Microbiol. Lett. 137:51-56(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from S.solfataricus strain
CC P1, but the culture was contaminated with S.acidocaldarius.
CC {ECO:0000305|PubMed:1658539}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY80783.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X58538; CAA41429.1; -; Genomic_DNA.
DR EMBL; X77509; CAA54643.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80783.1; ALT_INIT; Genomic_DNA.
DR PIR; S53703; S53703.
DR RefSeq; WP_048054401.1; NC_007181.1.
DR PDB; 5L3S; X-ray; 1.90 A; B/D/F/H=79-368.
DR PDB; 5L3W; X-ray; 2.40 A; A=69-368.
DR PDBsum; 5L3S; -.
DR PDBsum; 5L3W; -.
DR AlphaFoldDB; P27414; -.
DR SMR; P27414; -.
DR STRING; 330779.Saci_1462; -.
DR EnsemblBacteria; AAY80783; AAY80783; Saci_1462.
DR GeneID; 33345996; -.
DR KEGG; sai:Saci_1462; -.
DR PATRIC; fig|330779.12.peg.1406; -.
DR eggNOG; arCOG01227; Archaea.
DR HOGENOM; CLU_009301_3_4_2; -.
DR Proteomes; UP000001018; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome.
FT CHAIN 1..369
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101217"
FT REGION 20..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 262..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 320..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5L3W"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5L3W"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5L3W"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5L3S"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5L3W"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:5L3S"
SQ SEQUENCE 369 AA; 41889 MW; A31FD398698C6C97 CRC64;
MICFDRLKKA FSNFLDKISG EENKKEPETR QTDQLESKKE ETIQQQQNVQ QPQAENKIEQ
KQEKISVQTG QENKQENKRS FFDFLKYKTI KEDDLNDVIE ELRFQLLDSD VSYEVTEKIL
EDLKNNLIGK KVSRREEVEE IVINTLKKSI TEILTKNQKT DLIEKIRSSG KKPFVIIFFG
VNGVGKTTTI AKVVNMLKKN NLSTIIAASD TFRAAAQEQL AYHASKLEVQ LIRGKYGADP
ASVAFDAISF AKSRNIDVVL IDTAGRMHID SDLVEELKRV LRIAKPDFRI LILDSLAGSD
ALEQARHFEN NVGYDAVILT KVDADAKGGI ALSLAYELKK PVVYMGVGQN YDDLIPFSPD
WFVERIFSS
