FTSY_THEAQ
ID FTSY_THEAQ Reviewed; 304 AA.
AC P83749;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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};
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271 {ECO:0000312|EMBL:AAR28967.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6; 19-25 AND
RP 87-93, AND MUTAGENESIS OF ARG-17; LEU-18; ARG-86; LYS-87 AND LEU-88.
RX PubMed=12009409; DOI=10.1016/s0167-4838(02)00287-x;
RA Shepotinovskaya I.V., Freymann D.M.;
RT "Conformational change of the N-domain on formation of the complex between
RT the GTPase domains of Thermus aquaticus Ffh and FtsY.";
RL Biochim. Biophys. Acta 1597:107-114(2002).
RN [2] {ECO:0000305}
RP CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=14501130; DOI=10.1107/s0907444903016573;
RA Shepotinovskaya I.V., Focia P.J., Freymann D.M.;
RT "Crystallization of the GMPPCP complex of the NG domains of Thermus
RT aquaticus Ffh and FtsY.";
RL Acta Crystallogr. D 59:1834-1837(2003).
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 -!- INTERACTION:
CC P83749; O07347: ffh; NbExp=3; IntAct=EBI-1037899, EBI-1037906;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}.
CC -!- PTM: Sensitive to endogenous proteolytic cleavage between residues 18
CC and 19 and between residues 86 and 87.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; AY484668; AAR28967.1; -; Genomic_DNA.
DR RefSeq; WP_053767748.1; NZ_LHCI01000106.1.
DR PDB; 1OKK; X-ray; 2.05 A; D=2-304.
DR PDB; 1RJ9; X-ray; 1.90 A; A=1-304.
DR PDB; 2CNW; X-ray; 2.39 A; D/E/F=21-304.
DR PDB; 2IYL; X-ray; 2.10 A; D=21-304.
DR PDB; 2J7P; X-ray; 1.97 A; D/E=22-304.
DR PDB; 2Q9A; X-ray; 2.24 A; A/B=1-304.
DR PDB; 2Q9B; X-ray; 2.30 A; A/B=1-304.
DR PDB; 2Q9C; X-ray; 2.20 A; A/B=1-304.
DR PDB; 2XKV; EM; 13.50 A; D=2-304.
DR PDBsum; 1OKK; -.
DR PDBsum; 1RJ9; -.
DR PDBsum; 2CNW; -.
DR PDBsum; 2IYL; -.
DR PDBsum; 2J7P; -.
DR PDBsum; 2Q9A; -.
DR PDBsum; 2Q9B; -.
DR PDBsum; 2Q9C; -.
DR PDBsum; 2XKV; -.
DR AlphaFoldDB; P83749; -.
DR SMR; P83749; -.
DR IntAct; P83749; 2.
DR EvolutionaryTrace; P83749; -.
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 PANTHER; PTHR43134:SF7; PTHR43134:SF7; 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; 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; Direct protein sequencing;
KW GTP-binding; Membrane; Nucleotide-binding; Receptor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12009409"
FT CHAIN 2..304
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101147"
FT BINDING 109..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 255..258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT MUTAGEN 17
FT /note="R->Q: No effect on proteolysis; when associated with
FT M-18."
FT /evidence="ECO:0000269|PubMed:12009409"
FT MUTAGEN 18
FT /note="L->M: No effect on proteolysis; when associated with
FT Q-17."
FT /evidence="ECO:0000269|PubMed:12009409"
FT MUTAGEN 86
FT /note="R->Q: No effect proteolysis; when associated with Q-
FT 87 and I-88."
FT /evidence="ECO:0000269|PubMed:12009409"
FT MUTAGEN 87
FT /note="K->Q: No effect proteolysis; when associated with Q-
FT 86 and I-88."
FT /evidence="ECO:0000269|PubMed:12009409"
FT MUTAGEN 88
FT /note="L->I: No effect proteolysis; when associated with Q-
FT 86 and Q-87."
FT /evidence="ECO:0000269|PubMed:12009409"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2Q9C"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:2Q9C"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2Q9C"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2Q9C"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1RJ9"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1RJ9"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1RJ9"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2IYL"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:2Q9A"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2IYL"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2IYL"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1RJ9"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2Q9C"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1RJ9"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:1RJ9"
SQ SEQUENCE 304 AA; 33055 MW; 51881F90B4780536 CRC64;
MGFFDRLKAG LAKTRERLLK AIPWGGNLEE VLEELEMALL AADVGLSATE EILQEVRASG
RKDLKEAVKE KLVGMLEPDE RRATLRKLGF NPQKPKPVEP KGRVVLVVGV NGVGKTTTIA
KLGRYYQNLG KKVMFCAGDT FRAAGGTQLS EWGKRLSIPV IQGPEGTDPA ALAYDAVQAM
KARGYDLLFV DTAGRLHTKH NLMEELKKVK RAIAKADPEE PKEVWLVLDA VTGQNGLEQA
KKFHEAVGLT GVIVTKLDGT AKGGVLIPIV RTLKVPIKFV GVGEGPDDLQ PFDPEAFVEA
LLED
