FTSY_MYCTU
ID FTSY_MYCTU Reviewed; 422 AA.
AC P9WGD9; L0TDS3; P66842; Q10969;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=Rv2921c;
GN ORFNames=MTCY338.10c;
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, ACTIVITY REGULATION, INTERACTION WITH FFH/SRP, 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).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-236 AND ASP-367.
RC STRAIN=H37Rv;
RX PubMed=33412199; DOI=10.1016/j.ijbiomac.2020.12.182;
RA Shivangi X., Ekka M.K., Meena L.S.;
RT "Essential biochemical, biophysical and computational inputs on efficient
RT functioning of Mycobacterium tuberculosis H37Rv FtsY.";
RL Int. J. Biol. Macromol. 171:59-73(2021).
CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC proteins into the cytoplasmic membrane. Acts as a receptor for the
CC complex formed by the signal recognition particle (SRP) and the
CC ribosome-nascent chain (RNC) (By similarity). Most of the substrate
CC proteins are involved in stress regulation, lipid metabolism,
CC intermediary metabolism, and cell wall processes (PubMed:29361248).
CC Shows GTPase activity (PubMed:29361248, PubMed:33412199). Can also
CC hydrolyze ATP, UTP and CTP (PubMed:33412199). {ECO:0000255|HAMAP-
CC Rule:MF_00920, ECO:0000269|PubMed:29361248,
CC ECO:0000269|PubMed:33412199}.
CC -!- ACTIVITY REGULATION: The SRP-FtsY complex formation results in mutual
CC stimulation of their GTP hydrolysis activity (PubMed:29361248). GTPase
CC activity is stimulated by Mg(2+) or a high concentration of Mn(2+).
CC Increasing Mg(2+) decreases the activity (PubMed:33412199). GDP acts as
CC an inhibitor (PubMed:33412199). {ECO:0000269|PubMed:29361248,
CC ECO:0000269|PubMed:33412199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39.95 uM for GTP {ECO:0000269|PubMed:33412199};
CC KM=24.87 uM for ATP {ECO:0000269|PubMed:33412199};
CC Vmax=20.25 umol/min/mg enzyme {ECO:0000269|PubMed:33412199};
CC Vmax=12.23 umol/min/mg enzyme {ECO:0000269|PubMed:33412199};
CC Note=kcat is 0.012 sec(-1) for GTP hydrolysis (PubMed:33412199). kcat
CC is 0.007 sec(-1) for ATP hydrolysis (PubMed:33412199).
CC {ECO:0000269|PubMed:33412199};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:33412199};
CC Temperature dependence:
CC Optimum temperature is 25-37 degrees Celsius.
CC {ECO:0000269|PubMed:33412199};
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_00920, ECO:0000269|PubMed:29361248}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00920};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00920};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00920}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; AL123456; CCP45723.1; -; Genomic_DNA.
DR PIR; A70748; A70748.
DR RefSeq; NP_217437.1; NC_000962.3.
DR RefSeq; WP_003899541.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WGD9; -.
DR SMR; P9WGD9; -.
DR STRING; 83332.Rv2921c; -.
DR PaxDb; P9WGD9; -.
DR DNASU; 887205; -.
DR GeneID; 887205; -.
DR KEGG; mtu:Rv2921c; -.
DR TubercuList; Rv2921c; -.
DR eggNOG; COG0552; Bacteria.
DR OMA; GISDQFQ; -.
DR PhylomeDB; P9WGD9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00920; FtsY; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004390; SR_rcpt_FtsY.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134:SF7; PTHR43134:SF7; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00064; ftsY; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome.
FT CHAIN 1..422
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101139"
FT REGION 39..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 312..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 374..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT MUTAGEN 236
FT /note="K->A: Severely affects the affinity toward GTP and
FT causes a significant decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:33412199"
FT MUTAGEN 367
FT /note="D->A: Severely affects the affinity toward GTP and
FT causes a significant decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:33412199"
SQ SEQUENCE 422 AA; 44031 MW; C9B44AF200ECC346 CRC64;
MWEGLWIATA VIAALVVIAA LTLGLVLYRR RRISLSPRPE RGVVDRSGGY TASSGITFSQ
TPTTQPAERI DTSGLPAVGD DATVPRDAPK RTIADVHLPE FEPEPQAPEV PEADAIAPPE
GRLERLRGRL ARSQNALGRG LLGLIGGGDL DEDSWQDVED TLLVADLGPA ATASVVSQLR
SRLASGNVRT EADARAVLRD VLINELQPGM DRSIRALPHA GHPSVLLVVG VNGTGKTTTV
GKLARVLVAD GRRVVLGAAD TFRAAAADQL QTWAARVGAA VVRGPEGADP ASVAFDAVDK
GIAAGADVVL IDTAGRLHTK VGLMDELDKV KRVVTRRASV DEVLLVLDAT IGQNGLAQAR
VFAEVVDISG AVLTKLDGTA KGGIVFRVQQ ELGVPVKLVG LGEGPDDLAP FEPAAFVDAL
LG
