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Database: UniProt
Entry: B1C161_9FIRM
LinkDB: B1C161_9FIRM
Original site: B1C161_9FIRM 
ID   B1C161_9FIRM            Unreviewed;       327 AA.
AC   B1C161;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:EDS75116.1};
GN   ORFNames=CLOSPI_00944 {ECO:0000313|EMBL:EDS75116.1};
OS   Thomasclavelia spiroformis DSM 1552.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS75116.1, ECO:0000313|Proteomes:UP000004910};
RN   [1] {ECO:0000313|EMBL:EDS75116.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75116.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS75116.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75116.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2008) 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:EDS75116.1}.
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DR   EMBL; ABIK02000007; EDS75116.1; -; Genomic_DNA.
DR   RefSeq; WP_004608694.1; NZ_DS562844.1.
DR   AlphaFoldDB; B1C161; -.
DR   STRING; 428126.CLOSPI_00944; -.
DR   GeneID; 67387448; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_3_4_9; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000004910; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004910}.
FT   DOMAIN          295..308
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         210..214
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
FT   BINDING         274..277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   327 AA;  36013 MW;  6AA809F20ECAFAB7 CRC64;
     MGFFNKIKEK FVGKSAKQNE KYVAGLDRSN VTFSDRINEL AARFREINED YFEELENILI
     MSDVGVSMVM KIVDEIKNEV RIQNITDPKQ INDIIVDKMF VIYANDSVMT TKINYASEGL
     TVILMVGVNG AGKTTTIGKL ANRIVQDEGK KVMVAAGDTF RAGAIDQLAV WADRVGVEIV
     KGREGGDPSA VVFDALKQAK EKNVDVLICD TAGRLQNKVN LMKELEKMNR IIKREVPDAP
     HETLLVIDAT TGQNGVSQAV EFSKITDITG LVLTKMDGTA KGGIVLSIKD QLNIPVKFIG
     LGEGVDDLQE FDLDQYIYGL CKNLVEG
//
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