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Database: UniProt
Entry: K9XFG1_9CHRO
LinkDB: K9XFG1_9CHRO
Original site: K9XFG1_9CHRO 
ID   K9XFG1_9CHRO            Unreviewed;       484 AA.
AC   K9XFG1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=Glo7428_1858 {ECO:0000313|EMBL:AFZ30407.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30407.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ30407.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30407.1,
RC   ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-2012) 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; CP003646; AFZ30407.1; -; Genomic_DNA.
DR   RefSeq; WP_015188281.1; NC_019745.1.
DR   AlphaFoldDB; K9XFG1; -.
DR   STRING; 1173026.Glo7428_1858; -.
DR   KEGG; glp:Glo7428_1858; -.
DR   PATRIC; fig|1173026.3.peg.1977; -.
DR   eggNOG; COG0541; Bacteria.
DR   HOGENOM; CLU_009301_6_0_3; -.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000010476; 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:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 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:UP000010476};
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   REGION          382..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
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         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   484 AA;  52737 MW;  E704E76FEF7EDF9F CRC64;
     MFDALADRLE SAWKKLRGQD KITQSNIQEA LREVRRALLE ADVNLQVVKD FIAEVESHAQ
     GAEVIAGVRP DQQFIKIVYE ELVQVMGETN VPLAQAEQPP TIVLMAGLQG TGKTTATAKL
     ALHLRKLERS CMMVATDVYR PAAIDQLVTL GKQIEVPVFE MGSDANPVEI ARQGVERAKA
     EGVDTVIIDT AGRLQIDQDM MAELAQIKET VQPHEVLLVV DAMTGQEAAN LTRTFHDEIG
     ITGAILTKLD GDSRGGAALS VRQISGQPIK FVGVGEKVEA LQPFYPDRMA SRILGMGDVL
     TLVEKAQEEI DLADAAKMQE KIMAAKFDFT DFLKQMRLLK NMGSLGGIMK LIPGMNKLSE
     DQLKQGETQL KRAEAMINSM TAQERRDPDL LASSPSRRKR IANGSGYKEA DVNKLVGDFQ
     KMRSLMQQMT QGGFPGMPGM FGGMGDPLAA AGNRPSAPGW RGYSGGGTAK KKKKEKKKKG
     FGTL
//
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