SRP54_MYCTU
ID SRP54_MYCTU Reviewed; 525 AA.
AC P9WGD7; 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 46.
DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE Short=SRP {ECO:0000303|PubMed:22534010};
DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=Rv2916c;
GN ORFNames=MTCY338.04c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION AS A GTPASE, AND INTERACTION WITH 4.5S RNA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22534010; DOI=10.1016/j.micres.2012.03.002;
RA Palaniyandi K., Veerasamy M., Narayanan S.;
RT "Characterization of Ffh of Mycobacterium tuberculosis and its interaction
RT with 4.5S RNA.";
RL Microbiol. Res. 167:520-525(2012).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH FTSY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=29361248; DOI=10.1139/cjm-2017-0385;
RA Venkatesan A., Palaniyandi K., Sharma D., Bisht D., Narayanan S.;
RT "Characterization of FtsY, its interaction with Ffh, and proteomic
RT identification of their potential substrates in Mycobacterium
RT tuberculosis.";
RL Can. J. Microbiol. 64:243-251(2018).
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 (By similarity).
CC Most of the substrate proteins are involved in stress regulation, lipid
CC metabolism, intermediary metabolism, and cell wall processes
CC (PubMed:29361248). Shows GTPase activity (PubMed:22534010).
CC {ECO:0000255|HAMAP-Rule:MF_00306, ECO:0000269|PubMed:22534010,
CC ECO:0000269|PubMed:29361248}.
CC -!- ACTIVITY REGULATION: The SRP-FtsY complex formation results in mutual
CC stimulation of their GTP hydrolysis activity.
CC {ECO:0000269|PubMed:29361248}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY (PubMed:29361248). SRP is a
CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule
CC (PubMed:22534010). Can interact with FtsY in the absence of 4.5S RNA
CC (PubMed:29361248). {ECO:0000269|PubMed:22534010,
CC ECO:0000269|PubMed:29361248}.
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: Depletion of ffh (SRP) and ftsY results in
CC differential expression of 14 proteins. {ECO:0000269|PubMed:29361248}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; AL123456; CCP45718.1; -; Genomic_DNA.
DR PIR; D70747; D70747.
DR RefSeq; NP_217432.1; NC_000962.3.
DR RefSeq; WP_003414748.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WGD7; -.
DR SMR; P9WGD7; -.
DR STRING; 83332.Rv2916c; -.
DR PaxDb; P9WGD7; -.
DR DNASU; 888242; -.
DR GeneID; 45426903; -.
DR GeneID; 888242; -.
DR KEGG; mtu:Rv2916c; -.
DR TubercuList; Rv2916c; -.
DR eggNOG; COG0541; Bacteria.
DR OMA; DTAGRHK; -.
DR PhylomeDB; P9WGD7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..525
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101163"
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
