ID T5CJD2_HELPX Unreviewed; 843 AA.
AC T5CJD2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N411_04480 {ECO:0000313|EMBL:EQL57417.1};
OS Helicobacter pylori FD535.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191464 {ECO:0000313|EMBL:EQL57417.1, ECO:0000313|Proteomes:UP000015966};
RN [1] {ECO:0000313|EMBL:EQL57417.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL57417.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL57417.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL57417.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(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:EQL57417.1}.
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DR EMBL; AKHP02000019; EQL57417.1; -; Genomic_DNA.
DR RefSeq; WP_020982397.1; NZ_AKHP02000019.1.
DR AlphaFoldDB; T5CJD2; -.
DR PATRIC; fig|1191464.11.peg.1235; -.
DR Proteomes; UP000015966; 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 310..557
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 559..693
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 718..836
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 132..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..294
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 769
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 843 AA; 94379 MW; 16B15619C94A5963 CRC64;
MDDLQEIMED FLIEAFEMNE QLDQDLVELE HNPEDLDLLN RIFRVAHTIK GSSSFLNLNI
LTHLTHNMED VLNRARKGEI KITPDIMDVV LCSIDLMKTL LVTIRDTGSD TNNGKENEIE
EAVKQLQAIT SQNLEGAKET SGTKEAPQKE NKEENKEENK EEAKEENKEE NKEEAKEENK
EENKEEAKEE NKENKAKAPT AENSASDNPL ADEPDLDYTN MSAEEVEAEI ERLLNKRQEA
DKERRAQKKQ EAKPKQKVTP TKETPKTETL KTETPKAPKT ETKAKTKADT EENKAPSIGV
EQTVRVDVRR LDHLMNLIGE LVLGKNRLIR IYSDVEERYD 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 ITILEAANGL EGLEMLKNGD KIPDAILVDI EMPKMDGYTF
ASEVRKYNKF KNLPLIAVTS RVTKTDRMRG VESGMTEYIT KPYSGEYLTT VVKRSIKLEG
DQS
//
