ID A0A1G8QCN1_9BACI Unreviewed; 466 AA.
AC A0A1G8QCN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04490247_0534 {ECO:0000313|EMBL:SDJ02467.1};
OS Salimicrobium halophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=86666 {ECO:0000313|EMBL:SDJ02467.1, ECO:0000313|Proteomes:UP000199225};
RN [1] {ECO:0000313|EMBL:SDJ02467.1, ECO:0000313|Proteomes:UP000199225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4771 {ECO:0000313|EMBL:SDJ02467.1,
RC ECO:0000313|Proteomes:UP000199225};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEV01000001; SDJ02467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8QCN1; -.
DR STRING; 86666.SAMN04490247_0534; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000199225; 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: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 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}.
FT DOMAIN 426..439
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 341..345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT BINDING 405..408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ SEQUENCE 466 AA; 51714 MW; 3623F2EA9F88C2EE CRC64;
MGFFKKLKEK FTPIEVGEPV DHEKEDAEDV EAPAREEETG TETSEDRSRQ DDPSIDEATD
SDKGALELDE AEESEKLESP VTEETPELEE PETEETVELE APAQEKLEAP ETEEPEAKLQ
EPPSHESEEE WTEEELPEPV EDGEKVSIAE KFKKGLAKTR NSFSTKINDL VAKYREVDEE
FFEELEEVLI SADVGVHAVM ELIEELEMEV KRRNIKDTKE VREVISEKLV ELYYGEDDEE
EVEGLHEEEG DLTVYLFVGV NGVGKTTSIG KLAYQLKQEG KKVLLAAGDT FRAGAIEQLD
AWGKRVGVDV IKHNAGSDPA AVVYDGIQAA KSRKADVLIC DTAGRLQNKV NLMNELSKVK
KVISREIPEA PHEVLLTLDA TTGQNAMSQA KTFSEATDVT GIVLTKLDGT AKGGIILAIR
RELEIPVKLV GLGEGVNDLE TFDAHAFVYG LFADMIDDYE EETEKG
//
