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Database: UniProt
Entry: A0A101CST7_9FLAO
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Original site: A0A101CST7_9FLAO 
ID   A0A101CST7_9FLAO        Unreviewed;       317 AA.
AC   A0A101CST7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=AR687_12150 {ECO:0000313|EMBL:KUJ61683.1};
OS   Flavobacteriaceae bacterium CRH.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ61683.1, ECO:0000313|Proteomes:UP000053826};
RN   [1] {ECO:0000313|EMBL:KUJ61683.1, ECO:0000313|Proteomes:UP000053826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRH {ECO:0000313|EMBL:KUJ61683.1,
RC   ECO:0000313|Proteomes:UP000053826};
RA   Newman J.D., Miller J.R., Jacobs K.T.;
RT   "Genome Sequence of Flavobacterium sp. CHR.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|HAMAP-Rule:MF_00920};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00920};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}. Cytoplasm
CC       {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUJ61683.1}.
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DR   EMBL; LMAJ01000010; KUJ61683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101CST7; -.
DR   STRING; 1742859.AR687_12150; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000053826; Unassembled WGS sequence.
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 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}.
FT   DOMAIN          290..303
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   BINDING         123..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         205..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   317 AA;  34706 MW;  F0383342F6669A9F CRC64;
     MSFFKKLFST DKKETLDKSL EKSKTTFFSK LSKVVAGKSK VDDDVLDDLE EILVASDVGV
     NTTLKIISRI EKRVAEDKYL GTEELNQILR EEIAGLLSET NRGEATEFDI PKDKKPYVLM
     VVGVNGVGKT TTIGKLAYQF KKAGYKVVLG AADTFRAAAI DQLQVWADRV DVPIVRQNMG
     SDPASVAFDT LQSAVAQNAD IVIIDTAGRL HNKINLMNEL TKVKRVMQKV VADAPHDVLL
     VLDGSTGQNA FEQAKQFTAA TEVTSLAVTK LDGTAKGGVV IGISDQFQIP VKYIGVGEGI
     EDLQVFNKYE FVDSFFK
//
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