ID A0A2W6PLN6_9HELI Unreviewed; 803 AA.
AC A0A2W6PLN6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B6S12_08320 {ECO:0000313|EMBL:PZT47563.1};
OS Helicobacter valdiviensis.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1458358 {ECO:0000313|EMBL:PZT47563.1, ECO:0000313|Proteomes:UP000249746};
RN [1] {ECO:0000313|EMBL:PZT47563.1, ECO:0000313|Proteomes:UP000249746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBE14 {ECO:0000313|EMBL:PZT47563.1,
RC ECO:0000313|Proteomes:UP000249746};
RA Fresia P., Jara R., Sierra R., Ferres I., Greif G., Iraola G., Collado L.;
RT "Genomic and clinical evidence uncovers the enterohepatic species
RT Helicobacter valdiviensis as a potential human intestinal pathogen.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:PZT47563.1}.
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DR EMBL; NBIU01000028; PZT47563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W6PLN6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000249746; 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 CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000249746}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 247..516
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 518..652
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 677..795
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 132..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Polar 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 728
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 803 AA; 89304 MW; 1B0842087D3A5724 CRC64;
MDEMQEILED FLIEAFEMIE QLDQDLVELE NHPDDLDLLN RIFRVAHTIK GSGSFLNFSV
LTHLTHHMED VLNKARHGEL TITPDIMDVV LESIDYMKKL LSAIRDTGSD ANTGLEGEIE
GTISRLDAIS KGEAPSEAKE IPQEQVATTT TQAKEEAPQE PEEELDYANM SAEEVEKEIE
RLLNQRQEED KKKREEKRAR GEELDIQAPK EVQEEAKATQ ATPSPATPKT QEQPATPKPA
PKSSASKPQE ENKAPATAVE QTIRVDVKRL DSLMNLIGEL VLGKNRLIKI YNDVEERYEG
EKFLEELNQV VASVSMVTTD IQLAVMKTRM LPIGRVFNKF PRMVRDLSRE LGKNIDLVIS
GEETELDKSI VEEIGDPLVH LIRNACDHGI ESKEERIAAG KKEQGTVELK AYNEGNHIVV
EITDDGKGMN PEVLKAKAVE KGIISEREAD TMTDKEAYSL IFKAGFSTAK VVTNVSGRGV
GMDVVKTNIE KLNGIIDVES SFGEGTTLKL KIPLTLAIIQ SLLVGVQEEF YAIPLASVIE
TVRISQDEIY TVENKSVLRL RNEVLPLVRL ADIFGVDSVF DNSEQAYVVV IGLAENKIGI
IVDFLIGQEE VVIKSLGSYL KGTEGIAGAT IRGDGRVTLI VDIAAMMQMA KHVKVSINKL
IQESEAKHEK NSPSDYHVLI VDDSMTDRSI MKKSLKPLGI TLTEATNGLE ALDIVKNGDR
TFDAILIDIE MPKMDGYTLA GEIRKYAKFK NLPLIAVTSR TSKTDRMRGV ESGMTEYITK
PYSPEYLMNV VKRNINLTME VTE
//
