ID A0A853S683_9PROT Unreviewed; 769 AA. AC A0A853S683; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=AJ939_05285 {ECO:0000313|EMBL:OEW21263.1}; OS Campylobacter sp. BCW_6889. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=1903293 {ECO:0000313|EMBL:OEW21263.1}; RN [1] {ECO:0000313|EMBL:OEW21263.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCW_6889 {ECO:0000313|EMBL:OEW21263.1}; RA Weis A.M., Weimer B.C., Townsend A.K., Taff C.; RT "Campylobacter in American crows."; RL Submitted (SEP-2016) 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:OEW21263.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MJWZ01000055; OEW21263.1; -; Genomic_DNA. DR RefSeq; WP_070276355.1; NZ_MJWZ01000055.1. DR AlphaFoldDB; A0A853S683; -. DR Proteomes; UP000865665; 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}. FT DOMAIN 1..104 FT /note="HPt" FT /evidence="ECO:0000259|PROSITE:PS50894" FT DOMAIN 241..488 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 490..624 FT /note="CheW-like" FT /evidence="ECO:0000259|PROSITE:PS50851" FT DOMAIN 648..766 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT REGION 130..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 186..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 195..214 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 699 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 769 AA; 85273 MW; E7FBDF1EB4140E7B CRC64; MEDMQEILED FLVEAFELVE QIDHDLVELE SNPEDLELLN RIFRVAHTVK GSSSFLNFDV LTKLTHHMED VLNKARHGEL KITPDIMDVV LESIDRMKTL LNSIRDNGND TAIGMDIEPI CARLTAISEG ESPVAAKDSN EKSTLQVEPE APKQEIATPE PEVDINQLSD SEVEAEIERL LKVRKAEDQA RRAQKKQTTN AAPKPTNNTA NKPAESGEKK VPASGSNASS MDQTIRVEVK RLDHLMNLIG ELVLGKNRLL KIYDDVEERY EGEKFLEELN QVVSQLSIIT TDVQLAVMKT RMQPIAKVFN KFPRVVRDLS RELGKQIELE ITGEETELDK SIVEEIGDPI MHMIRNSCDH GVEDPATRAA NGKPEKGIVQ LKAYNEGNHI VVEITDDGKG LDPNGLKAKA IEKNLITERE ADQMTDKEAF ALIFKPGFST AAKVTNVSGR GVGMDVVKTN IEKLNGVIEI DSELGKGSSF KLKIPLTLAI IQSLLVGTQE EFYAIPLASV LETVRVPIDD IYTIEGKNVL RLRDEVLSLV RLSDVFGVKQ VLESGDQTYV VVIGVAESKL GIIVDTLVGQ EEIVIKSMGD YLQNIQGIAG ATIRGDGRVT LIIDVGAMMD MAKEIKVDIK AQLESSAKKP KEQPSDYKVL IVDDSKMDRT LMQKALEPLG VSLVEATNGV EALNIIKSGE HDIDAMLIDI EMPRMDGYTL AGEIRKYSKY RNLPLIAVTS RTSKTDRLRG VEVGMTEYIT KPYSPEYLEN VVRKNLKLG //