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Database: UniProt
Entry: Q39WG0_GEOMG
LinkDB: Q39WG0_GEOMG
Original site: Q39WG0_GEOMG 
ID   Q39WG0_GEOMG            Unreviewed;       351 AA.
AC   Q39WG0;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 118.
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   ECO:0000313|EMBL:ABB31414.1};
GN   OrderedLocusNames=Gmet_1176 {ECO:0000313|EMBL:ABB31414.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31414.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB31414.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB31414.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
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|ARBA:ARBA00035577, ECO:0000256|HAMAP-
CC         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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}.
CC       Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00920}.
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DR   EMBL; CP000148; ABB31414.1; -; Genomic_DNA.
DR   RefSeq; WP_004513442.1; NC_007517.1.
DR   AlphaFoldDB; Q39WG0; -.
DR   STRING; 269799.Gmet_1176; -.
DR   KEGG; gme:Gmet_1176; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_3_0_7; -.
DR   OMA; GISDQFQ; -.
DR   Proteomes; UP000007073; Chromosome.
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   CDD; cd17874; FtsY; 1.
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; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43134:SF1; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00920}; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007073}.
FT   DOMAIN          324..337
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          19..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         157..164
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         239..243
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         303..306
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   351 AA;  38311 MW;  B43D2D752E466700 CRC64;
     MAEEKKGFIK GLWNKIAGAE GAEENPIPEQ RTEVAEHPVQ AEEPEERKPG LFERLRQGLS
     KTRDSLVGRI DRLVLGKKEI DADTLEELEE ILITADIGVQ TTVELIRILE ERLSRNELND
     GAALRQTLKD EILKRLSRDV RPLAVDSASP FVIMVIGVNG VGKTTTIGKL AARFSREGKK
     VVLAAGDTFR AAAAEQLEIW GERTGCDVVR HKEGADPSAV VFDGIKAAVA RKADVLIVDT
     AGRLHTKVNL MEELKKVRRI MDREIPGAPH ETLLVLDAAT GQNALSQAKL FKEAAEVTGI
     ALTKLDGTAK GGIVAAICNE FRIPVRYIGV GEGVDDLRDF DPAEFVDALF Q
//
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