ID A0A318GZY4_9BURK Unreviewed; 742 AA.
AC A0A318GZY4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7444_11965 {ECO:0000313|EMBL:PXW93554.1};
OS Sphaerotilus hippei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=744406 {ECO:0000313|EMBL:PXW93554.1, ECO:0000313|Proteomes:UP000247811};
RN [1] {ECO:0000313|EMBL:PXW93554.1, ECO:0000313|Proteomes:UP000247811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 566 {ECO:0000313|EMBL:PXW93554.1,
RC ECO:0000313|Proteomes:UP000247811};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:PXW93554.1}.
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DR EMBL; QJJS01000019; PXW93554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318GZY4; -.
DR OrthoDB; 8577169at2; -.
DR Proteomes; UP000247811; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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 InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000247811};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 489..606
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 642..742
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 139..166
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 204..234
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 538
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 681
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 742 AA; 80775 MW; ED997C083EE673C4 CRC64;
MAFPARRRWL GGAAAGVVLA LAGVAFVQWQ QLRLLNEAVS AESDNIGFQS LQFESEFLGV
RDRLRGAGWP VPARELDDLR ERWELFVSRV DLMEQGSMSR RLAHYPDHQL LMGDIRALVA
DGDRFLPDGA PQPVTQAALQ DFRARIETLR HRVHDLMLKV TSLESEQVGV RNAAVRRQNL
IAIGLTLFQA LLAVAVTWLA VRHFQREQQR RQELERLNLQ LTRAREQAEQ ASQAKSEFLA
TMSHELRTPF NGMLGMIELA QDGPLDAQQS RQLQAAASSA EHLLALLNDI LDASKLEADA
LVLALVPTSP GQLAQELVQM VAPQARDKGL ELAWHVDEQL PAWVQVDAMR LRQILLNLLT
NALKFTERGR IDLNVSVLPA PPGPVQQPVI RFAVADTGIG MDADAVGRLF ERFSQADASI
SRRFGGTGLG LEISRRLARL MGGDIDVSST PGQGSVFTLW LPVSEARAPA PAPGPVPAVS
PPGLGSGLDV LVVDDHPVNR DFMEAVLVSL GHRPRCCDNG QRAIEAVRSR VPDVVFMDLH
MPVMDGWQAT RALRALHGPA SRVPIVALSA DAFAQTHARA LDEGMDEFLS KPVRRQELAM
VLARLCPRAP AVDAGRIAAP VAPPLAELID DSVVAELGEI FSGPACQAML GRFFADRAAS
YASTLAALEA GAAQRWSAPA HALKGAAGTL GFMRLAELAQ RIEVDGAAWT PERARQEARL
LQEAWIATQQ LCAVRGLLDE TG
//
