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Database: UniProt
Entry: Q5P734_AROAE
LinkDB: Q5P734_AROAE
Original site: Q5P734_AROAE 
ID   Q5P734_AROAE            Unreviewed;       386 AA.
AC   Q5P734;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 120.
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:CAI06877.1};
GN   ORFNames=ebA1393 {ECO:0000313|EMBL:CAI06877.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06877.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI06877.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI06877.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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). Interaction with SRP-RNC leads to the
CC       transfer of the RNC complex to the Sec translocase for insertion into
CC       the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the
CC       dissociation of the SRP-FtsY complex into the individual components.
CC       {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. SRP is a ribonucleoprotein
CC       composed of Ffh and a 4.5S RNA molecule. {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; CR555306; CAI06877.1; -; Genomic_DNA.
DR   RefSeq; WP_011236605.1; NC_006513.1.
DR   AlphaFoldDB; Q5P734; -.
DR   STRING; 76114.ebA1393; -.
DR   KEGG; eba:ebA1393; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_4_2_4; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000006552; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   NCBIfam; TIGR00064; ftsY; 1.
DR   PANTHER; PTHR43134:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43134; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:CAI06877.1};
KW   Cell division {ECO:0000313|EMBL:CAI06877.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   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:UP000006552}.
FT   DOMAIN          351..364
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         185..192
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         266..270
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         330..333
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   386 AA;  41043 MW;  861177BC77509F58 CRC64;
     MFGFLRKKPA KPDAVEDKAQ PDEIPAAEPA LDQAEPVAEA VQPAPPAEVG PDLEASLEAP
     FETPVPLGAE IAKPGAKRSW SERLKAGLSR TRQQLGGGLA SLFGRRKIDE ELLEELEATL
     LMADCGVEAT QHLLGELRKR WKRDRLETAD QLQKALADEL HAILLPLEEP LDVSGHSPYI
     IMIAGVNGSG KTTSIGKLAK YFQAQGRSVL LAAGDTFRAA AREQLMTWGE RNNVTVIAQD
     GGDSAAVIFD AINAAKARRI DVVLADTAGR LPTQLHLMDE IAKVKRVIAK ASPSGPHEVL
     LVLDANIGQN ALAQVKAFDS AIGVTGLVVT KLDGTAKGGV VAAIARQYPR PLRFIGVGEG
     IDDLQPFKAR EFVDALFDTN GAGSAA
//
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