ID Q7VRI6_BLOFL Unreviewed; 308 AA.
AC Q7VRI6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Cell division protein FtsY {ECO:0000313|EMBL:CAD83302.1};
GN Name=ftsY {ECO:0000313|EMBL:CAD83302.1};
GN OrderedLocusNames=Bfl627 {ECO:0000313|EMBL:CAD83302.1};
OS Blochmannia floridanus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83302.1, ECO:0000313|Proteomes:UP000002192};
RN [1] {ECO:0000313|EMBL:CAD83302.1, ECO:0000313|Proteomes:UP000002192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC {ECO:0000256|ARBA:ARBA00008531}.
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DR EMBL; BX248583; CAD83302.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VRI6; -.
DR STRING; 203907.Bfl627; -.
DR KEGG; bfl:Bfl627; -.
DR eggNOG; COG0552; Bacteria.
DR HOGENOM; CLU_009301_3_0_6; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000002192; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 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 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: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; 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 cycle {ECO:0000313|EMBL:CAD83302.1};
KW Cell division {ECO:0000313|EMBL:CAD83302.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170}.
FT DOMAIN 280..293
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
SQ SEQUENCE 308 AA; 34482 MW; 4F32AC3DEA0D06B2 CRC64;
MDTKFTLFNK LKTSLLNTRK KIGDSIFDIF HNRIVDHDTI NIIKNQLIKS DVNIQTTQKI
INNFKKNTFL NMNLNSKSIY EIIHHSMLQI MKPVEKPLFI TNQQPFVILV IGVNGVGKTT
TVGKLAYHYR SQNKSVMIAA GDTKRAAAID QLITFTKNID SISIIANYST SDSASIIFNA
MQKALSQNIN ILIIDTAGRL QNNIHNIQEL QKIQQTIKKI QPNAPHETIL VLDSNIGQNS
INQLKTFHST ITITGIIMTK LDGSSKGGVL LSISNCFSIP IRYLGIGQNL EDLQIFNATE
FIEAILTK
//
