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Database: UniProt
Entry: A0A0U5MX10_9PROT
LinkDB: A0A0U5MX10_9PROT
Original site: A0A0U5MX10_9PROT 
ID   A0A0U5MX10_9PROT        Unreviewed;       454 AA.
AC   A0A0U5MX10;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 32.
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:CUW37345.1};
GN   ORFNames=XM1_0276 {ECO:0000313|EMBL:CUW37345.1};
OS   Magnetospirillum sp. XM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW37345.1, ECO:0000313|Proteomes:UP000063191};
RN   [1] {ECO:0000313|Proteomes:UP000063191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wang Y.;
RL   Submitted (DEC-2015) 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; LN997848; CUW37345.1; -; Genomic_DNA.
DR   RefSeq; WP_068428533.1; NZ_LN997848.1.
DR   AlphaFoldDB; A0A0U5MX10; -.
DR   STRING; 1663591.XM1_0276; -.
DR   KEGG; magx:XM1_0276; -.
DR   PATRIC; fig|1663591.3.peg.278; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000063191; Chromosome I.
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   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};
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          268..281
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         189..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         247..250
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   454 AA;  48788 MW;  E698969473F18943 CRC64;
     MFESLSSRLG KVFEKLTGRG ALSEADVTEA LREVRVALLE ADVALSVVKE FIGRVKARAV
     GAEVIKSVTP GQMVVKIVHD ELIATLGTKG NELSLSAVPP VVILMVGLQG SGKTTTSAKI
     ALKLKKEKKK VLLASLDVYR PAAQQQLQIL AGQAEVGSLP IVMGEMPVAI SKRALDVGRK
     EGYDVVILDT AGRLHIDQEL MAEVAAVRDA TKPTETLLVT DAMTGQDAVT LAREFNEKVG
     VTGIVLTRID GDARGGAALS MRAITGRPIK FLGAGEKLDA LEVFHPDRIA GRILGMGDVV
     GLVEKAMETL DQEEAERLAK RMEKGKFDLD DMRKQFAQVR KMGDLKGILG MLPGIGKMAG
     ALKDANIDNK MVARQEAIIS SMTKAERKNP DLIKASRKKR IATGAGVEVQ DVNKLLKQYQ
     QMADMMKKVG KLGQKGLMRH GIGGLLPPGM KFGR
//
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