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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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