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PDTAS_MYCTU
ID   PDTAS_MYCTU             Reviewed;         501 AA.
AC   P9WGL5; L0TDI0; O05846; Q7D5W7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Probable sensor histidine kinase PdtaS;
DE            EC=2.7.13.3;
GN   Name=pdtaS; OrderedLocusNames=Rv3220c;
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, AND AUTOPHOSPHORYLATION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16026786; DOI=10.1016/j.febslet.2005.06.043;
RA   Morth J.P., Gosmann S., Nowak E., Tucker P.A.;
RT   "A novel two-component system found in Mycobacterium tuberculosis.";
RL   FEBS Lett. 579:4145-4148(2005).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
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 PdtaR/PdtaS.
CC       Autophosphorylates, probably on a histidine residue, and transfers its
CC       phosphate group to PdtaR. {ECO:0000269|PubMed:16026786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- PTM: Autophosphorylated.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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DR   EMBL; AL123456; CCP46036.1; -; Genomic_DNA.
DR   PIR; E70596; E70596.
DR   RefSeq; NP_217736.1; NC_000962.3.
DR   RefSeq; WP_003416886.1; NZ_NVQJ01000003.1.
DR   PDB; 2YKF; X-ray; 2.00 A; A=1-303.
DR   PDB; 2YKH; X-ray; 2.78 A; A/B=1-303.
DR   PDBsum; 2YKF; -.
DR   PDBsum; 2YKH; -.
DR   AlphaFoldDB; P9WGL5; -.
DR   SMR; P9WGL5; -.
DR   STRING; 83332.Rv3220c; -.
DR   PaxDb; P9WGL5; -.
DR   DNASU; 888801; -.
DR   GeneID; 45427213; -.
DR   GeneID; 888801; -.
DR   KEGG; mtu:Rv3220c; -.
DR   TubercuList; Rv3220c; -.
DR   eggNOG; COG3920; Bacteria.
DR   OMA; GSIAIVH; -.
DR   PhylomeDB; P9WGL5; -.
DR   PHI-base; PHI:3621; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:MTBBASE.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MTBBASE.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IDA:MTBBASE.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR   Gene3D; 3.30.450.280; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR038424; H_kinase_PdtaS_GAF_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR022066; PdtaS_GAF.
DR   InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR   Pfam; PF12282; H_kinase_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Two-component regulatory system.
FT   CHAIN           1..501
FT                   /note="Probable sensor histidine kinase PdtaS"
FT                   /id="PRO_0000386596"
FT   DOMAIN          300..495
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         303
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   HELIX           4..11
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           16..36
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          38..45
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           81..88
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           141..158
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:2YKH"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           195..203
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           215..219
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           226..240
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          256..267
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   STRAND          270..280
FT                   /evidence="ECO:0007829|PDB:2YKF"
FT   HELIX           282..285
FT                   /evidence="ECO:0007829|PDB:2YKF"
SQ   SEQUENCE   501 AA;  54012 MW;  DF099B268388AD00 CRC64;
     MSTLGDLLAE HTVLPGSAVD HLHAVVGEWQ LLADLSFADY LMWVRRDDGV LVCVAQCRPN
     TGPTVVHTDA VGTVVAANSM PLVAATFSGG VPGREGAVGQ QNSCQHDGHS VEVSPVRFGD
     QVVAVLTRHQ PELAARRRSG HLETAYRLCA TDLLRMLAEG TFPDAGDVAM SRSSPRAGDG
     FIRLDVDGVV SYASPNALSA YHRMGLTTEL EGVNLIDATR PLISDPFEAH EVDEHVQDLL
     AGDGKGMRME VDAGGATVLL RTLPLVVAGR NVGAAILIRD VTEVKRRDRA LISKDATIRE
     IHHRVKNNLQ TVAALLRLQA RRTSNAEGRE ALIESVRRVS SIALVHDALS MSVDEQVNLD
     EVIDRILPIM NDVASVDRPI RINRVGDLGV LDSDRATALI MVITELVQNA IEHAFDPAAA
     EGSVTIRAER SARWLDVVVH DDGLGLPQGF SLEKSDSLGL QIVRTLVSAE LDGSLGMRDA
     RERGTDVVLR VPVGRRGRLM L
 
 
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