SRP54_MYCTO
ID SRP54_MYCTO Reviewed; 525 AA.
AC P9WGD6; L0TDR8; P66844; Q10963;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Signal recognition particle protein {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=MT2984;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- 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 -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK47310.1; -; Genomic_DNA.
DR PIR; D70747; D70747.
DR RefSeq; WP_003414748.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGD6; -.
DR SMR; P9WGD6; -.
DR EnsemblBacteria; AAK47310; AAK47310; MT2984.
DR GeneID; 45426903; -.
DR KEGG; mtc:MT2984; -.
DR PATRIC; fig|83331.31.peg.3224; -.
DR HOGENOM; CLU_009301_6_0_11; -.
DR Proteomes; UP000001020; 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: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; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11564; PTHR11564; 1.
DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 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; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00959; ffh; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..525
FT /note="Signal recognition particle protein"
FT /id="PRO_0000428380"
FT REGION 437..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..469
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:0000255|HAMAP-Rule:MF_00306"
FT BINDING 196..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 254..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ SEQUENCE 525 AA; 55002 MW; 36F6227BC367817C CRC64;
MFESLSDRLT AALQGLRGKG RLTDADIDAT TREIRLALLE ADVSLPVVRA FIHRIKERAR
GAEVSSALNP AQQVVKIVNE ELISILGGET RELAFAKTPP TVVMLAGLQG SGKTTLAGKL
AARLRGQGHT PLLVACDLQR PAAVNQLQVV GERAGVPVFA PHPGASPESG PGDPVAVAAA
GLAEARAKHF DVVIVDTAGR LGIDEELMAQ AAAIRDAINP DEVLFVLDAM IGQDAVTTAA
AFGEGVGFTG VALTKLDGDA RGGAALSVRE VTGVPILFAS TGEKLEDFDV FHPDRMASRI
LGMGDVLSLI EQAEQVFDAQ QAEEAAAKIG AGELTLEDFL EQMLAVRKMG PIGNLLGMLP
GAAQMKDALA EVDDKQLDRV QAIIRGMTPQ ERADPKIINA SRRLRIANGS GVTVSEVNQL
VERFFEARKM MSSMLGGMGI PGIGRKSATR KSKGAKGKSG KKSKKGTRGP TPPKVKSPFG
VPGMPGLAGL PGGLPDLSQM PKGLDELPPG LADFDLSKLK FPGKK
