TCRY_MYCTU
ID TCRY_MYCTU Reviewed; 475 AA.
AC O69729; L0TGH0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Probable sensor histidine kinase TcrY;
DE EC=2.7.13.3;
GN Name=tcrY; OrderedLocusNames=Rv3764c;
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 FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT "Deletion of two-component regulatory systems increases the virulence of
RT Mycobacterium tuberculosis.";
RL Infect. Immun. 71:1134-1140(2003).
RN [3]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19962420; DOI=10.1016/j.biochi.2009.11.009;
RA Bhattacharya M., Biswas A., Das A.K.;
RT "Interaction analysis of TcrX/Y two component system from Mycobacterium
RT tuberculosis.";
RL Biochimie 92:263-272(2010).
RN [4]
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).
CC -!- FUNCTION: Member of the two-component regulatory system TcrY/TcrX.
CC Activates TcrX by phosphorylation. {ECO:0000269|PubMed:12595424,
CC ECO:0000269|PubMed:19962420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:19962420};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for ATP {ECO:0000269|PubMed:19962420};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19962420}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Cells lacking TcrX and TcrY show an increase in
CC virulence in mouse model of infection, with significantly shorter
CC survival times. {ECO:0000269|PubMed:12595424}.
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DR EMBL; AL123456; CCP46591.1; -; Genomic_DNA.
DR PIR; E70801; E70801.
DR RefSeq; NP_218281.1; NC_000962.3.
DR RefSeq; WP_010886181.1; NZ_KK339374.1.
DR AlphaFoldDB; O69729; -.
DR SMR; O69729; -.
DR STRING; 83332.Rv3764c; -.
DR PaxDb; O69729; -.
DR DNASU; 886094; -.
DR GeneID; 886094; -.
DR KEGG; mtu:Rv3764c; -.
DR PATRIC; fig|83332.111.peg.4186; -.
DR TubercuList; Rv3764c; -.
DR eggNOG; COG2205; Bacteria.
DR InParanoid; O69729; -.
DR OMA; AMNRVES; -.
DR PhylomeDB; O69729; -.
DR SABIO-RK; O69729; -.
DR PHI-base; PHI:3616; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0005509; F:calcium ion binding; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..475
FT /note="Probable sensor histidine kinase TcrY"
FT /id="PRO_0000412200"
FT TOPO_DOM 1..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..238
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 253..466
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 256
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 475 AA; 50344 MW; 5CE7FC3E7D3A7BAF CRC64;
MGITAATEMA LRRHLVAQLD NQLGGTSYRS VLMYPEKMPR PPWRHETHNY IRSGPGPRFL
DAPGQPAGMV AAVVSDGTTV AAGYLTGSGS RAALTSTGRS QLERIAGSRT PLTLDLDGLG
RYRVLAAPSR NGHDVIVTGL SMGNVDATML QMLIIFGIVT VIALVAATTA GIVIIKRALA
PLRRVAQTAS EVVDLPLDRG EVKLPVRVPE PDANPSTEVG QLGSALNRML DHIAAALSAR
QASETCVRQF VADASHELRT PLAAIRGYTE LTQRIGDDPE AVAHAMSRVA SETERITRLV
EDLLLLARLD SGRPLERGPV DMSRLAVDAV SDAHVAGPDH QWALDLPPEP VVIPGDAARL
HQVVTNLLAN ARVHTGPGTI VTTRLSTGPT HVVLQVIDNG PGIPAALQSE VFERFARGDT
SRSRQAGSTG LGLAIVSAVV KAHNGTITVS SSPGYTEFAV RLPLDGWQPL ESSPR
