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Database: UniProt
Entry: D3F1D7_CONWI
LinkDB: D3F1D7_CONWI
Original site: D3F1D7_CONWI 
ID   D3F1D7_CONWI            Unreviewed;       444 AA.
AC   D3F1D7;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306};
DE            EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00306};
DE   AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306};
GN   Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306};
GN   OrderedLocusNames=Cwoe_3683 {ECO:0000313|EMBL:ADB52100.1};
OS   Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS   100937 / ID131577).
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB52100.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|EMBL:ADB52100.1, ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RX   PubMed=21304704;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA   Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA   Hugenholtz P.;
RT   "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL   Stand. Genomic Sci. 2:212-219(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC       proteins into the cytoplasmic membrane. Binds to the hydrophobic signal
CC       sequence of the ribosome-nascent chain (RNC) as it emerges from the
CC       ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic
CC       membrane where it interacts with the SRP receptor FtsY.
CC       {ECO:0000256|HAMAP-Rule:MF_00306}.
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_00306};
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_00306}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}.
CC       Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_00306}.
CC   -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is
CC       responsible for interactions with the ribosome, the central G domain,
CC       which binds GTP, and the C-terminal M domain, which binds the RNA and
CC       the signal sequence of the RNC. {ECO:0000256|HAMAP-Rule:MF_00306}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|HAMAP-Rule:MF_00306}.
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DR   EMBL; CP001854; ADB52100.1; -; Genomic_DNA.
DR   RefSeq; WP_012935151.1; NC_013739.1.
DR   AlphaFoldDB; D3F1D7; -.
DR   STRING; 469383.Cwoe_3683; -.
DR   KEGG; cwo:Cwoe_3683; -.
DR   eggNOG; COG0541; Bacteria.
DR   HOGENOM; CLU_009301_6_0_11; -.
DR   OMA; PIKFAGV; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000008229; Chromosome.
DR   GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
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; cd18539; SRP_G; 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   Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1.
DR   HAMAP; MF_00306; SRP54; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR   InterPro; IPR004780; SRP.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   NCBIfam; TIGR00959; ffh; 1.
DR   PANTHER; PTHR11564:SF7; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   Pfam; PF02978; SRP_SPB; 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   SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00306};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00306}; Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW   ECO:0000256|HAMAP-Rule:MF_00306}.
FT   DOMAIN          269..282
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   BINDING         107..114
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         190..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         248..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   444 AA;  48911 MW;  DC6408D276AA1736 CRC64;
     MFDSLAEKLQ ATLSDVRSRG TLTEDDVNAA MREIRLALLE ADVNFKVVKR FTNAVKERAL
     GSDVIGQLNP GQQVVKIVND ELAELMGGES AELRFSSSPP TVILMAGLQG SGKTTATAKL
     ARLLREQNRS SVAVAACDVY RPAAVEQLIT VGARAGADVY ERGTDADPVE IAKWARERAE
     REGKDVLIVD TAGRLHVDEN LMKELAEIKR VTNPTNVLLV VDAMTGQDAV NVAEQFAEVV
     QFDGVVMSKL DGDARGGAAL SVKSVTGKPI LFASTGEKLD QFERFHPDRM AQRILGMGDV
     MTLIEKAESQ FDETQAKELE RKIRKSEFGL DDFLDQLRQV RRLGPLQSLL GMMPGLGGHQ
     LRNLRVDERE FDRIQAIILS MTAEERRNPD IIKGSRRIRI ARGSGTNVQA VKALIRQFGQ
     MQRLMKSMQS GKMPDIGALM RQAR
//
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