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Database: UniProt
Entry: N1UZ96_9MICC
LinkDB: N1UZ96_9MICC
Original site: N1UZ96_9MICC 
ID   N1UZ96_9MICC            Unreviewed;       514 AA.
AC   N1UZ96;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=D477_016535 {ECO:0000313|EMBL:EMY33119.1};
OS   Arthrobacter crystallopoietes BAB-32.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY33119.1, ECO:0000313|Proteomes:UP000010729};
RN   [1] {ECO:0000313|EMBL:EMY33119.1, ECO:0000313|Proteomes:UP000010729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-32 {ECO:0000313|EMBL:EMY33119.1,
RC   ECO:0000313|Proteomes:UP000010729};
RX   PubMed=23833141;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT   Revealing Genes for Bioremediation.";
RL   Genome Announc. 1:e00452-13(2013).
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}.
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:EMY33119.1}.
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DR   EMBL; ANPE02000199; EMY33119.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1UZ96; -.
DR   Proteomes; UP000010729; Unassembled WGS sequence.
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:UP000010729};
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          277..290
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          442..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..476
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107..114
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         198..202
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         256..259
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   514 AA;  55797 MW;  79EE1638274B1DE9 CRC64;
     MFNSLSDRLA STFKNLRGKG RLSEADVDAT VREIRRALLD ADVAVSVVRE FTAHVRERAL
     SEEVSAALNP GQQVVKIVND ELVRILGGET RRIRLAKNPP TVIMLAGLQG AGKTTLAGKL
     SKWLKGQGHS PILVAADLQR PNAVTQLQVN GQRAGVPVFA PHPGVQSDFE EVTGDPVTVA
     RDGVAEARAK LHDVVIVDTA GRLGIDAEMM QQAADIRAAV NPDEVLFVID AMIGQDAVNT
     AQAFNEGVDF TGVVLSKLDG DARGGAALSV ASVTGKPVMF ASTGESLDDF EIFHPDRMAN
     RILDMGDILS LIEQAEKSWD KGEAERMAKK FADQEDFTLE DFLAQMQQIR KMGSMKKMLT
     MMPGAAGMRQ QLENFDEREI DRVEAIVRSM TPHERLAPKI INGSRRARIA RGSGVHVSEV
     NGLLERFGQA QKMMKKMAQG GGIPGMPGMA GPGGFGGPRK ASRLPRAKRR PVRATRQRLP
     RSSARPKSAG PMRGRRCPRA QPSASSRRTS IRRR
//
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