ID G2IWT9_PSEUL Unreviewed; 772 AA.
AC G2IWT9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=NH8B_3045 {ECO:0000313|EMBL:BAK77831.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK77831.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; AP012224; BAK77831.1; -; Genomic_DNA.
DR RefSeq; WP_014088008.1; NC_016002.1.
DR AlphaFoldDB; G2IWT9; -.
DR STRING; 748280.NH8B_3045; -.
DR KEGG; pse:NH8B_3045; -.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_011685_0_0_4; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000001274; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAK77831.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001274};
KW Transferase {ECO:0000313|EMBL:BAK77831.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 283..355
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 359..411
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 543..758
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 772 AA; 86478 MW; 366504E4C651E01F CRC64;
MPKSRSPRFL LLTTVGSLLA LITALSGIVY LVYRDWMEGQ RDSLIQEVLW LDQSLRLHLE
THREWAENAA NDVSGLRING YQFQQSARLL LRENPELLEA ERVDARGRIL WDTRRVNLPG
DVLSGAAHDA LWRASKLMRA AYGEAYRGRD GKYRFDMAVP IIVEGEYVGG IRLVYQMEGL
LYNQVPWWIA SKYLISIQDL GGKVLASRFD EAEQPGTLQY QISFDPPGHG LTLRAVEYRS
AMGLTLPVLV VAVVTLVLAL LYSVWRIRRH IRERSAAERA LELEMSLRQA MEDSMKSGLM
ALSASGEIVR VNRAFCAMSG FSENELVGQS PPHSFWPTNE YPLLHDTIAA VLRGFQPEHG
FEVPFVTKNG EAFEVRLFAT PLVERDGSQR GWICSMYDIT ELKKKRLALN ASHQRFLTVL
NGLDAGVCVT DKGGSQLLYA NPTFSHLWMK DEPDADCCLL LPRLPDGDEE GAENQHLEFT
SDGGSNWFQI HRRRIEWVDG QEAWLSILTD VTELRQREAR ERAQEERFQN TSRLIAMGEM
ASSLAHELNQ PLSAINTYSS GLQRRLPPDL ELPKGVREAI QAISEQARRA GQIVNSIRAF
VKKHAPQLEL ADPAKVVGRA IGLAEPMVVK HGVNLLLQPS ESVCRLEMDP VLIEQVLLNL
IKNAVEAMRD AETRRPQVTV RYGADAGYWR VEVADNGPGL SDSIRSNLFT PFYSSKPDGL
GIGLNICRSI VEFHRGQFGV ERSAGGGCAF WFTLPVAALE REQKTAPAGA VR
//
