位置:首页 > 蛋白库 > FTSY_MYCMS
FTSY_MYCMS
ID   FTSY_MYCMS              Reviewed;         400 AA.
AC   Q6MTB9;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=MSC_0489;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 88-400.
RX   PubMed=16343944; DOI=10.1016/j.jsb.2005.10.003;
RA   Gariani T., Samuelsson T., Sauer-Eriksson A.E.;
RT   "Conformational variability of the GTPase domain of the signal recognition
RT   particle receptor FtsY.";
RL   J. Struct. Biol. 153:85-96(2006).
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   ---------------------------------------------------------------------------
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; BX293980; CAE77117.1; -; Genomic_DNA.
DR   RefSeq; NP_975475.1; NC_005364.2.
DR   PDB; 1ZU4; X-ray; 1.95 A; A=88-400.
DR   PDB; 1ZU5; X-ray; 2.40 A; A/B=88-400.
DR   PDBsum; 1ZU4; -.
DR   PDBsum; 1ZU5; -.
DR   AlphaFoldDB; Q6MTB9; -.
DR   SMR; Q6MTB9; -.
DR   STRING; 272632.MSC_0489; -.
DR   EnsemblBacteria; CAE77117; CAE77117; MSC_0489.
DR   KEGG; mmy:MSC_0489; -.
DR   PATRIC; fig|272632.4.peg.529; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_3_3_14; -.
DR   OMA; GISDQFQ; -.
DR   EvolutionaryTrace; Q6MTB9; -.
DR   Proteomes; UP000001016; 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   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.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome.
FT   CHAIN           1..400
FT                   /note="Signal recognition particle receptor FtsY"
FT                   /id="PRO_0000416703"
FT   REGION          12..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         192..199
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         278..282
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         342..345
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   HELIX           92..107
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           114..126
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           131..144
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           151..167
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:1ZU5"
FT   STRAND          186..193
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           198..211
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           226..236
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          244..247
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           256..269
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          273..278
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           286..301
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          309..316
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           321..330
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   TURN            331..333
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           344..346
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           352..360
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          364..368
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   STRAND          376..378
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           381..388
FT                   /evidence="ECO:0007829|PDB:1ZU4"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:1ZU4"
SQ   SEQUENCE   400 AA;  45730 MW;  E8ABED8D9BD99CAD CRC64;
     MGFWAKLKEK LTKKTNQVEQ DEPILDQQDQ QDQQEEQEQI IEKEIEQIKE NKIKKTKTSE
     TKKQEKPIET LKEKKKREKQ KEKDKKVEKA MLKSAFNFSK DIKKLSKKYK QADDEFFEEL
     EDVLIQTDMG MKMVLKVSNL VRKKTKRDTS FENIKDALVE SLYQAYTDND WTNKKYRIDF
     KENRLNIFML VGVNGTGKTT SLAKMANYYA ELGYKVLIAA ADTFRAGATQ QLEEWIKTRL
     NNKVDLVKAN KLNADPASVV FDAIKKAKEQ NYDLLLIDTA GRLQNKVNLM AELEKMNKII
     QQVEKSAPHE VLLVIDATTG QNGVIQAEEF SKVADVSGII LTKMDSTSKG GIGLAIKELL
     NIPIKMIGVG EKVDDLLAFD IDQYIVHLSS GFMQGDEVEK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025