ID K7YSW4_HELPX Unreviewed; 821 AA.
AC K7YSW4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HPAKL117_04960 {ECO:0000313|EMBL:AFX91387.1};
OS Helicobacter pylori Aklavik117.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055531 {ECO:0000313|EMBL:AFX91387.1, ECO:0000313|Proteomes:UP000010079};
RN [1] {ECO:0000313|EMBL:AFX91387.1, ECO:0000313|Proteomes:UP000010079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aklavik117 {ECO:0000313|EMBL:AFX91387.1};
RX PubMed=25883278;
RA Kersulyte D., Bertoli M.T., Tamma S., Keelan M., Munday R., Geary J.,
RA Veldhuyzen van Zanten S., Goodman K.J., Berg D.E.;
RT "Complete Genome Sequences of Two Helicobacter pylori Strains from a
RT Canadian Arctic Aboriginal Community.";
RL Genome Announc. 3:0-0(2015).
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; CP003483; AFX91387.1; -; Genomic_DNA.
DR RefSeq; WP_015086057.1; NC_019560.1.
DR AlphaFoldDB; K7YSW4; -.
DR KEGG; hpya:HPAKL117_04960; -.
DR PATRIC; fig|1055531.3.peg.1015; -.
DR HOGENOM; CLU_000650_3_6_7; -.
DR Proteomes; UP000010079; Chromosome.
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 Kinase {ECO:0000313|EMBL:AFX91387.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:AFX91387.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 290..537
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 539..673
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 698..816
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 132..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..274
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 749
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 821 AA; 91813 MW; ADE8AF78FFBE9390 CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LRSIDLMKTL LVTIRDTGSD TNNGKENEIE
EAVKQLQAIT SQNLEGAKET SGTKEAPKKE NQEEVKKEAK KENIEENTEE NQENKAKAPT
AKDFASDNPL ADEPDLDYTN MSAEEVEAEI ERLLNKRQEA DKERRAQKKQ ETKPKQEVAP
KTETHKTETP KTETPKAPKT ETKAKAKADT EENKAPSIGV EQTVRVDVRR LDHLMNLIGE
LVLGKNRLIR IYGDVEERYD GEKFLEELNQ VVSSISAVTT DLQLAVMKTR MQPVGKVFNK
FPRMVRDLSR ELGKSIELII EGEETELDKS IVEEIGDPLI HIIRNSCDHG IEPLEERRRL
NKPETGKVQL SAYNEGNHIV IKISDDGKGL DPVMLKEKAI EKGVISERDA EGMSDREAFN
LIFKPGFSTA KVVSNVSGRG VGMDVVKTNI EKLNGIIEID SEVGVGTTQK LKIPLTLAII
QALLVGVQEE YYAIPLSSVL ETVRISQDEI YTVDGKSVLR LRDEVLSLVR LSDIFKVDAI
LESNSDVYVV IIGLADQKIG VIVDYLIGQE EVVIKSLGYY LKNTRGIAGA TVRGDGKITL
IVDVGAMMDM AKSIKVNITT LMNESENTKS KNSPSDYIVL AIDDSSTDRA IIRKCLKPLG
ITLLEATNGL EGLEMLKNGD KTPDAILVDI EMPKMDGYTF ASEVRKYNKF KNLPLIAVTS
RVTKTDRMRG VESGMTEYIT KPYSGEYLTT IVKRSIKLEG E
//
