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NTRYL_RICTY
ID   NTRYL_RICTY             Reviewed;         599 AA.
AC   Q68WC5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Putative sensor histidine kinase NtrY-like;
DE            EC=2.7.13.3;
GN   OrderedLocusNames=RT0603;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system RT0603/RT0550.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU04067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017197; AAU04067.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014419450.1; NC_006142.1.
DR   AlphaFoldDB; Q68WC5; -.
DR   SMR; Q68WC5; -.
DR   STRING; 257363.RT0603; -.
DR   EnsemblBacteria; AAU04067; AAU04067; RT0603.
DR   KEGG; rty:RT0603; -.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   OMA; SKFARMP; -.
DR   OrthoDB; 692375at2; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; IPR045671; NtrY-like_N.
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   Pfam; PF19312; NtrY_N; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..599
FT                   /note="Putative sensor histidine kinase NtrY-like"
FT                   /id="PRO_0000282376"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          307..361
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          378..589
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         381
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   599 AA;  67324 MW;  751F55A1EA765265 CRC64;
     MLSYLKQNLC FYLSSKILIL ALAISAIVSA CTTFYVISLE AKNFSTIIGF LLIDLAIFLI
     LGILLTQKFF SKNNDNDSSR LQNRIVIAFS LVAAIPTIIV SVFSVYFFNL SVKAWFDKKI
     STVLDQSVIV AETYIAEHKV QLKETALAVA EDLSDMYYDL IHNPALFTKT LNTEADMRSL
     DEAIVLNKST NTIVANSYLS FSLSFATIPA HLIKKADLGE PVEVKSDPTK IRMLIKLKEY
     NDVYLLVGRL VDNKIIDHID ATNGAAAEYN SLKNEIDNIQ IKFSIMFIFI ALLLLFVAIN
     FGVLFTAQIV KPIKKLVTAT DKVKDGDLTV QVPENEVDKD EIGTLYVAFN RMIKQLSRQQ
     RDLVIAQRAM AWSDVAKKVA HEIKNPLTPI LLASERLLKK FSAEIKDKSE FESYLKMIIR
     HTNDIKNIVS EFVLFARLPA PKFTKSELVY LVKHIIEARK LLNDNIVYTC DSNVDQFDFM
     CDATQINQVM INVLKNAEES IEGQEFGRID VILDIKDDFI NVIVMDNGKG FPPELIGKAT
     ESYVTTSSKG MGVGLAIVKR IVEEHCGVLD IANREDKGAI IDIKFDLKEL HLKVRRSCG
 
 
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