ID T2STK5_HELPX Unreviewed; 810 AA.
AC T2STK5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L931_03555 {ECO:0000313|EMBL:EQD94839.1};
OS Helicobacter pylori PZ5024.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1337391 {ECO:0000313|EMBL:EQD94839.1, ECO:0000313|Proteomes:UP000015645};
RN [1] {ECO:0000313|EMBL:EQD94839.1, ECO:0000313|Proteomes:UP000015645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PZ5024 {ECO:0000313|EMBL:EQD94839.1,
RC ECO:0000313|Proteomes:UP000015645};
RX PubMed=24051318;
RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT Regions of Low and High Gastric Cancer Risk in Colombia.";
RL Genome Announc. 1:e00736-13(2013).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQD94839.1}.
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DR EMBL; ASYS01000353; EQD94839.1; -; Genomic_DNA.
DR AlphaFoldDB; T2STK5; -.
DR PATRIC; fig|1337391.3.peg.1543; -.
DR Proteomes; UP000015645; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 277..524
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 526..660
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 685..803
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 133..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 736
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 810 AA; 90466 MW; 354E38C7C222B34B CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LRSIDLMKTL LVTIRDTGSD TNNGKENEIE
EVVKKLQAIT SQNLEGAKET SGTKEAPEKE VKEEIKEKAK EEVKANKTPT TENPTSDNPL
ADEPDLDYAN MSAEEVEAEI ERLLNKRQEA DKERRAQKKQ EDQAKPKQEV APAKETPKTE
TPKAPKTETK AKAKADTEEN KAPSIGVEQT VRVDVRRLDH LMNLIGELVL GKNRLIRIYS
DVEERYDGEK FLEELNQVVS SISAVTTDLQ LAVMKTRMQP VGKVFNKFPR MVRDLSRELG
KSIELIIEGE ETELDKSIVE EIGDPLIHII RNSCDHGIEP LEERRRLNKP ETGKVQLSAY
NEGNHIVIKI SDDGKGLDPV MLKEKAIEKG VISERDAESM SDREAFNLIF KPGFSTAKVV
SNVSGRGVGM DVVKTNIEKL NGIIEIDSEV GVGTTQKLKI PLTLAIIQAL LVGVQEEYYA
IPLSSVLETV RISQDEIYTV DGKSVLRLRD EVLSLVRLSD IFKVDAILES NSDVYVVIIG
LADQKIGVIV DYLIGQEEVV IKSLGYYLKN TRGIAGATVR GDGKITLIVD VGAMMEMAKS
IKVNITTLMN ESENTKSKNS PSDYVVLAID DSSTDRAIIR KCLKPLGITL LEATNGLEGL
EMLKNGDKIP DAILVDIEMP KMDGYTFASE VRKYNKFKNL PLIAVTSRVT KTDRMRGVES
GMTEYITKPY SGEYLTTVVK RSIKLEGDQS
//
