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Database: UniProt
Entry: A0A0M0GQU7_9BACI
LinkDB: A0A0M0GQU7_9BACI
Original site: A0A0M0GQU7_9BACI 
ID   A0A0M0GQU7_9BACI        Unreviewed;       329 AA.
AC   A0A0M0GQU7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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   ECO:0000313|EMBL:TYS53908.1};
GN   ORFNames=AF331_06665 {ECO:0000313|EMBL:KON92133.1}, FZC83_11795
GN   {ECO:0000313|EMBL:TYS53908.1};
OS   Rossellomorea marisflavi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189381 {ECO:0000313|EMBL:KON92133.1, ECO:0000313|Proteomes:UP000037405};
RN   [1] {ECO:0000313|Proteomes:UP000037405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14235 jcm11544.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KON92133.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 11544 {ECO:0000313|EMBL:KON92133.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:TYS53908.1, ECO:0000313|Proteomes:UP000322997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH108_3D {ECO:0000313|EMBL:TYS53908.1,
RC   ECO:0000313|Proteomes:UP000322997};
RA   Olmedo-Alvarez G.;
RT   "Bacillus genomes from the desert of Cuatro Cienegas, Coahuila.";
RL   Submitted (AUG-2019) 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:KON92133.1}.
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DR   EMBL; LGUE01000001; KON92133.1; -; Genomic_DNA.
DR   EMBL; VTEQ01000003; TYS53908.1; -; Genomic_DNA.
DR   RefSeq; WP_053427321.1; NZ_VTEQ01000003.1.
DR   AlphaFoldDB; A0A0M0GQU7; -.
DR   STRING; 189381.GCA_900166615_02943; -.
DR   GeneID; 42291615; -.
DR   PATRIC; fig|189381.12.peg.1479; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000037405; Unassembled WGS sequence.
DR   Proteomes; UP000322997; 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: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; 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 cycle {ECO:0000313|EMBL:KON92133.1};
KW   Cell division {ECO:0000313|EMBL:KON92133.1};
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:UP000037405}.
FT   DOMAIN          294..307
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   BINDING         127..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         209..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         273..276
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   329 AA;  36109 MW;  2A691EDF83E86CB2 CRC64;
     MSFFKKLKDK FTQSSDSVTG KFKDGLSKTR SNFTTKVNDL VARYRKIDEE FFEELEEILI
     GADVGFDTVM ELIDELKLEV KRRNISDPVE VQSVISEKLV DIYQGDAEVS SELNIQEGEL
     TVLLFVGVNG VGKTTTIGKM AHMLKSEGKN VILAAGDTFR AGAIEQLEVW GERVGVPVIK
     QGAGSDPAAV MYDAVQSAKA KKADILICDT AGRLQNKVNL MKELEKVKRV IEREVPGAPH
     EVLLVLDATT GQNAMVQAKT FKEATDVSGI VLTKLDGTAK GGIVLAIRNE LDIPVKFVGL
     GEQMDDLQPF DAEKYVYGLF SNEVDNNEE
//
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