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Database: UniProt
Entry: A0A238K9Z7_9RHOB
LinkDB: A0A238K9Z7_9RHOB
Original site: A0A238K9Z7_9RHOB 
ID   A0A238K9Z7_9RHOB        Unreviewed;       502 AA.
AC   A0A238K9Z7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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   ECO:0000313|EMBL:SMX39224.1};
GN   ORFNames=MAA8898_01943 {ECO:0000313|EMBL:SMX39224.1};
OS   Maliponia aquimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Maliponia.
OX   NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX39224.1, ECO:0000313|Proteomes:UP000207598};
RN   [1] {ECO:0000313|EMBL:SMX39224.1, ECO:0000313|Proteomes:UP000207598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX39224.1,
RC   ECO:0000313|Proteomes:UP000207598};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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. Interaction
CC       with FtsY leads to the transfer of the RNC complex to the Sec
CC       translocase for insertion into the membrane, the hydrolysis of GTP by
CC       both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into
CC       the individual components. {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. SRP is a ribonucleoprotein
CC       composed of Ffh and a 4.5S RNA molecule. {ECO:0000256|HAMAP-
CC       Rule:MF_00306}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515}. Cytoplasm {ECO:0000256|HAMAP-
CC       Rule:MF_00306}. Note=The SRP-RNC complex is targeted to the cytoplasmic
CC       membrane. {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; FXYF01000004; SMX39224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238K9Z7; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000207598; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:UP000207598};
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          270..283
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          482..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         191..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         249..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   502 AA;  53412 MW;  99542EA8F169FED2 CRC64;
     MFENLSERLG GVFDRLTKQG ALTEDDVRTA LREVRVALLE ADVSLPVARQ FIKAVEKKAT
     GSAVTKSITP GQQVVKIVHD ELIAVLAGEG EPGKLRIDSP PAPILMVGLQ GGGKTTTTAK
     LAKRLKEREG KKVLMASLDV NRPAAMEQLA ILGKQIGVDT LPIVKGEDPV AIAKRTKTQA
     GLGGYDVYML DTAGRLSIDD ELMAQVEAVR DVANPRETLL VVDGLTGQDA VHTAENFDNR
     IGITGVVLTR MDGDGRGGAA LSMRAVTGKP IKFVGLGEKM EALETFEPER VAGRILGMGD
     IVALVEKAQA TLEAEQAERM MKRFQKGQFN MNDLKMQLDQ MIKMGGMEGM MSMLPGMGKM
     AKQLDGAGID DKILKQQIAL INSMTKLERA NPQVLQASRK KRIAAGAGME GADLNKLLKM
     QRQMSDMMKK MGKMGKGGML KQAMRGMFGG KGGLPPEMAQ GMDPKALEAA AKQMGKGLPG
     GLPGFGGGAA LPPGLSGLGK KK
//
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