ID J0P9N6_HELPX Unreviewed; 822 AA.
AC J0P9N6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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:EJB95302.1};
GN ORFNames=HPHPP1_1335 {ECO:0000313|EMBL:EJB95302.1};
OS Helicobacter pylori Hp P-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992072 {ECO:0000313|EMBL:EJB95302.1, ECO:0000313|Proteomes:UP000004015};
RN [1] {ECO:0000313|EMBL:EJB95302.1, ECO:0000313|Proteomes:UP000004015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-1 {ECO:0000313|EMBL:EJB95302.1,
RC ECO:0000313|Proteomes:UP000004015};
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:EJB95302.1}.
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DR EMBL; AKPI01000005; EJB95302.1; -; Genomic_DNA.
DR RefSeq; WP_000342381.1; NZ_AKPI01000005.1.
DR AlphaFoldDB; J0P9N6; -.
DR PATRIC; fig|992072.3.peg.1299; -.
DR Proteomes; UP000004015; 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:EJB95302.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EJB95302.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 289..536
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 538..672
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 697..815
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 133..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..273
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 748
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 822 AA; 91837 MW; 78C427CBA56F18A1 CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LRSIDLMKTL LVTIRDTGSD TNNGKENEIE
EVVKKLQAIT SQNLEGAKET SGTKEAPEKE VKKENKKENQ TETKAPTTEN PTSDNPLADE
PDLDYANMSA EEVEAEIERL LNKRQEADKE RRAQKKQEDQ AKPKQEVAPA KETPKTETPK
TETPKTETPK TETPKAPKTE TKAKAKADTE ENKAPSIGVE QTVRVDVRRL DHLMNLIGEL
VLGKNRLIRI YSDVEERYDG EKFLEELNQV VSSISAVTTD LQLAVMKTRM QPVGKVFNKF
PRMVRDLSRE LGKSIELIIE GEETELDKSI VEEIGDPLIH IIRNSCDHGI EPLEERRRLN
KPETGKVQLS AYNEGNHIVI KISDDGKGLD PVMLKEKAIE KGVISERDAE SMSDREAFNL
IFKPGFSTAK VVSNVSGRGV GMDVVKTNIE KLNGIIEIDS EVGVGTTQKL KIPLTLAIIQ
ALLVGVQEEY YAIPLSSVLE TVRINQDEIY TVDGKSVLRL RDEVLSLVRL SDIFKVDAIL
ESNSDVYVVI IGLADQKIGV IVDYLIGQEE VVIKSLGYYL KNTRGIAGAT VRGDGKITLI
VDVGAMMEMA KSIKVNITTL MNESENTKSK NSPSDYVVLA IDDSSTDRAI IRKCLKPLGI
TLLEATNGLE GLEMLKNGDK IPDAILVDIE MPKMDGYTFA SEVRKYNKFK NLPLIAVTSR
VTKTDRMRGV ESGMTEYITK PYSGEYLTTV VKRSIKLEGD QS
//
