ID A9C1I2_DELAS Unreviewed; 1044 AA.
AC A9C1I2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Daci_6017 {ECO:0000313|EMBL:ABX38645.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38645.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX38645.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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};
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DR EMBL; CP000884; ABX38645.1; -; Genomic_DNA.
DR AlphaFoldDB; A9C1I2; -.
DR STRING; 398578.Daci_6017; -.
DR KEGG; dac:Daci_6017; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3300; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_35_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.30.450.20; PAS domain; 3.
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; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF03707; MHYT; 2.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABX38645.1};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Transferase {ECO:0000313|EMBL:ABX38645.1};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 20..47
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 93..110
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 21..213
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 264..316
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 392..466
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 469..521
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 536..562
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 591..643
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 661..877
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 896..1017
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 947
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1044 AA; 114915 MW; 9EDD465CCDB7000B CRC64;
MNWDEIFVLG WAPHPQWFQW LHPGLVALSV VVAVATSMMA MQIAGLARNA ASPRIRRTGV
LTGAFCLGAG IWAMHFIGML AFVPCTFGDY DPWITALSML PSMLASWLAL TLMVRPRLSA
QALVGGGVLM GLGIGSMHYI GMAAAQTWSL MLYDPWGVLL SVIVAATMAM LSLWVRFRLG
NTGRLWPTLV AGIVMGLAIS CMHYAGLYAL RLKPGIDALA QQEAPTHALL VFSIVGVVVL
VFGLVLAVNM TLRYRQIYRQ VQRSESRLRA VVDTAVDGIV MIDGRGSIVS FNGAAERLLG
WTAQEVLGRS ASLLMPASGC DGEGGSLEKQ LAAGFAGLLG SSRDVHALHK DGTQIAVRLA
VGRVAIAGDP LFVGFVTDIR ERRQMLQSLR RSEEQYRTLI NNVPGTTFRC LYDGKWTPLL
LSRSIKELTG WTEQDFTDGL TGWDRLIHAE DRDRLEAAVS HSLSRRQTYN ADYRLLHRDG
STRWVSETGR GVFNEHDELT WIDGVIMDQT AARARNAEFE GTVRAIDLSL ATIEYDLLGQ
VLRANRNFLD LFGYRLDEVA GRHHGMFCEP GYAHTPEHEQ FWRRLAEGEF QAGEFLRCGR
EGRRIWVQAT YNPIRDADGR PYKIVKLLTD ISAQRKLAQE LVLAKEHAEA AAAARSTFLA
NMSHEIRTPM NAIIGFTEAL RETALQPTQA RYLDTVHYAA RSMLRLLNDI LDTAKLDKGA
VELEIEDFSV RELCQQILAS LRITADRKGL DLRLDYDPHT PAALRGDGMR VQQILVNLLG
NAVKFTERGH VLLRVRYEQG VLQLDVHDTG IGIAPEKIHR IFDPFAQADA STTRRFGGTG
LGTTISRQLA ELMGGSIQLH STVGVGTVFE VRLPLPVGEN QLPERGAVSR GLPPLHILAV
DDVPENLELL QINFSSQNHQ MALAHDGAEA LRRVQAQEPP FDVVLMDLQM PGMDGLAAAR
AIRVWERQLQ RRPVPIVALS ASVLEKDRSD ASAAGMDGFA SKPLDMARLQ AEIARLLSLQ
VALKEARPPA PASAQAGLPD VTVD
//
