ID A0A2S8YKZ8_9PSED Unreviewed; 926 AA.
AC A0A2S8YKZ8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-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=CQZ98_06315 {ECO:0000313|EMBL:PRA58255.1};
OS Pseudomonas sp. MYb115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA58255.1, ECO:0000313|Proteomes:UP000239970};
RN [1] {ECO:0000313|EMBL:PRA58255.1, ECO:0000313|Proteomes:UP000239970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb115 {ECO:0000313|EMBL:PRA58255.1,
RC ECO:0000313|Proteomes:UP000239970};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-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:PRA58255.1}.
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DR EMBL; PCQM01000003; PRA58255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8YKZ8; -.
DR Proteomes; UP000239970; 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; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; 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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PRA58255.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PRA58255.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..926
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015413352"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 405..625
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 643..765
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 793..912
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 697
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 842
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 926 AA; 102021 MW; 1EAAC9E9E39D9588 CRC64;
MRWLRNAIGL CVTLLTLLCM LPAQAGAQGS GWAVLFDDQG ALQLSDIRST RYTNQFSPIE
LDRITAANPG GALWLRFQLN PGKHEQLLRI FAPDLAQLDL YVLDGDTLVE QSHNGSDQPL
SARPLPSTDL MVPLPQREQP LDVYLRLVSE HQLRPYITLQ SAVMTAANQT QTLIYGLLFG
CIAMLILHNF TRYAYTRSQT CLWLAACEAL LMLGMLQLLN LAGPWLPDWS ALRSPAAYLA
LLLTAPCGLM FTYRFFTPRG PHPLNKLLLG DILLISLCSL LMLFVDTLPL NLMTFALVAL
AGLSMLFVSA FHWQKGYRPA RFFVMAMLVF NAGTLIILPA LLGLTLVAPQ GLITTLLALI
GLSGLLMGVS LSERQRSIME SRFSISRDLA ASNAEINAKA EFLAKISHEI RTPMNGVLGM
TELLLGTPLS VKQRDYVQTI HSAGNELLTL INEILDISKL ESGQIELDDV QFDLNALVED
CLSIFRAKAE QQNVELISFV QPQVPRVISG DPTRLRQTLL SLLENAMKNT EEGEILIVVA
LDERTTTPRL RIAVQDSGEP MDAEERELLM HAELHSKNFL AATRLGGNLG LVIARRLVLM
MHGEFGIKCG SNRGSTLWLT LPLDPDRLEH PTSDLDGPLQ DARVLVVDDN DTCRKVLVQQ
CSAWGLNVSA VSSGKEALAL LRTKAHLRDY FDVVLLDQNM PGMTGMQLAA KIKEDPSLNH
DILLIMLTGI SNAPSKIIAR NAGIKRILAK PVAGYTLKTT LADELNQRNK GPAVPPALPG
KVPVEVSVPS DFRILVAEDN SISTKVIRGM LGKLNLQPDT ASNGEEALKA MKAQRYDLVL
MDCEMPILDG FSATQQLRAW EVGNQRSRTP VVALTAHILA EHKERARQAG MDGHMAKPVE
LSQLRELIEH WVAQRDQLVQ SSTQPS
//
