ID SRP54_STRMU Reviewed; 516 AA.
AC Q54431; P96469;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE EC=3.6.5.4 {ECO:0000255|HAMAP-Rule:MF_00306};
DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=SMU_1060;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JH1005;
RA Gutierrez J.A., Cvitkovitch D.G., Brady L.J., Hamilton I.R., Hillman J.D.,
RA Bleiweis A.S.;
RT "Ffh of Streptococcus mutans is involved in acidurance.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
RC STRAIN=JH1005;
RX PubMed=8763945; DOI=10.1128/jb.178.14.4166-4175.1996;
RA Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA Bleiweis A.S.;
RT "Insertional mutagenesis and recovery of interrupted genes of Streptococcus
RT mutans by using transposon Tn917: preliminary characterization of mutants
RT displaying acid sensitivity and nutritional requirements.";
RL J. Bacteriol. 178:4166-4175(1996).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=NG8;
RX PubMed=16293689; DOI=10.1073/pnas.0508778102;
RA Hasona A., Crowley P.J., Levesque C.M., Mair R.W., Cvitkovitch D.G.,
RA Bleiweis A.S., Brady L.J.;
RT "Streptococcal viability and diminished stress tolerance in mutants lacking
RT the signal recognition particle pathway or YidC2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17466-17471(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_00306};
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. {ECO:0000255|HAMAP-
CC Rule:MF_00306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}.
CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00306}.
CC -!- DISRUPTION PHENOTYPE: Doubling time increases for growth under
CC nonstress conditions, unable to initiate growth at pH 5.0 and under
CC 3.5% NaCl salt stress. Double deletions of Ffh and FtsY, Ffh and scRNA,
CC or Ffh and YidC2 are barely able to grow in the absence of stress.
CC {ECO:0000269|PubMed:16293689}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; U88582; AAB48050.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58758.1; -; Genomic_DNA.
DR EMBL; U48883; AAC44500.1; -; Genomic_DNA.
DR RefSeq; NP_721452.1; NC_004350.2.
DR RefSeq; WP_002262280.1; NC_004350.2.
DR AlphaFoldDB; Q54431; -.
DR SMR; Q54431; -.
DR STRING; 210007.SMU_1060; -.
DR KEGG; smu:SMU_1060; -.
DR PATRIC; fig|210007.7.peg.947; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_9; -.
DR OrthoDB; 9804720at2; -.
DR PhylomeDB; Q54431; -.
DR Proteomes; UP000002512; 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; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..516
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101167"
FT REGION 383..405
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:0000255|HAMAP-Rule:MF_00306"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT CONFLICT 49
FT /note="V -> A (in Ref. 3; AAC44500)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="T -> I (in Ref. 1; AAB48050)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="K -> E (in Ref. 1; AAB48050)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="K -> N (in Ref. 1; AAB48050)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="E -> G (in Ref. 1; AAB48050)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="T -> A (in Ref. 1; AAB48050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57071 MW; 4712AB8EA64E7A8F CRC64;
MAFESLTERL QGVFKNLRGK RKLSEKDVQE VTKEIRLALL EADVALPVVK EFIKRVRKRA
VGHEVIDTLD PSQQIIKIVN EELTAVLGSE TAEIEKSSKI PTIIMMVGLQ GAGKTTFAGK
LANKLVKEEN ARPLMIAADI YRPAAIDQLK TLGQQINVPV FDMGTEHSAV EIVSQGLAQA
KENRNDYVLI DTAGRLQIDE KLMTELRDIK ALANPNEILL VVDSMIGQEA ANVAREFNQQ
LEVTGVILTK IDGDTRGGAA LSVRQITGKP IKFTGTGEKI TDIETFHPDR MSSRILGMGD
LLTLIEKASQ DYDEQKSAEL AEKMRENSFD FNDFIEQLDQ VQNMGSMEDI LKMIPGMANN
PALANVKVDE GEIARKRAIV SSMTPEEREN PDLLTPSRRR RIASGSGNTF VNVNKFIKDF
NQAKKMMQGV MSGDMNKVMK QMGINPNNMP KNMDSSALEG MMGQGGMPDM SELSGTNMDV
SQMFGGGLKG KVGEFAMKQS MKKMAKRMKK AKKRKK
//
