ID K2KHB1_HELPX Unreviewed; 800 AA.
AC K2KHB1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:EKE94986.1};
GN ORFNames=OUS_0870 {ECO:0000313|EMBL:EKE94986.1};
OS Helicobacter pylori R056a.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145118 {ECO:0000313|EMBL:EKE94986.1, ECO:0000313|Proteomes:UP000006748};
RN [1] {ECO:0000313|EMBL:EKE94986.1, ECO:0000313|Proteomes:UP000006748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R056a {ECO:0000313|EMBL:EKE94986.1,
RC ECO:0000313|Proteomes:UP000006748};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(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:EKE94986.1}.
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DR EMBL; AMOY01000006; EKE94986.1; -; Genomic_DNA.
DR RefSeq; WP_000342323.1; NZ_AMOY01000006.1.
DR AlphaFoldDB; K2KHB1; -.
DR PATRIC; fig|1145118.3.peg.860; -.
DR Proteomes; UP000006748; 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 Kinase {ECO:0000313|EMBL:EKE94986.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EKE94986.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 267..514
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 516..650
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 675..793
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 132..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..251
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 726
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 800 AA; 89284 MW; 444008E89F09C96C CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LRSIDLMKTL LVTIRDTGSD TNNGKENEIE
EAVKQLQAIT SQNLEGAKET SGTKEAPKEI KEEIKEKTKE EVKANKTPTA ENPASDNPLA
DEPDLDYANM SAEEVEAEIE RLLNKRQEAD KERRAQKKQE AKQEVTPTKE TPKAPKTETK
AKAKADTEEN KAPSIGVEQT VRVDVRRLDH LMNLIGELVL GKNRLIRIYS DVEERYDGEK
FLEELNQVVS SISAVTTDLQ LAVMKTRMQP VGKVFNKFPR MVRDLSRELG KSIELIIEGE
ETELDKSIVE EIGDPLIHII RNSCDHGIEP LEERRRLNKP ETGKVQLSAY NEGNHIVIKI
SDDGKGLDPV MLKEKAVEKG VISERDAEGM SDREAFNLIF KPGFSTAKVV SNVSGRGVGM
DVVKTNIEKL NGIIEIDSEV GVGTTQKLKI PLTLAIIQAL LVGVQEEYYA IPLSSVLETV
RISQDEIYTV DGKSVLRLRD EVLSLVRLSD IFKVDAILES NSDVYVVIIG LADQKIGVIV
DYLIGQEEVV IKSLGYYLKN TRGIAGATVR GDGKITLIVD VGAMMDMAKS IKVNITTLMN
ESENTKSKNS PSDYIVLAID DSSTDRAIIR KCLKPLGITL LEATNGLEGL EMLKNGDKIP
DAILVDIEMP KMDGYTFASE VRKYNKFKNL PLIAVTSRVT KTDRMRGVES GMTEYITKPY
SGEYLTTVVK RSIKLEGDQS
//
