ID A0A087N6H5_9SPHN Unreviewed; 630 AA.
AC A0A087N6H5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=IL54_0094 {ECO:0000313|EMBL:KFL44728.1};
OS Sphingobium sp. ba1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL44728.1, ECO:0000313|Proteomes:UP000029094};
RN [1] {ECO:0000313|EMBL:KFL44728.1, ECO:0000313|Proteomes:UP000029094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT Sphingobium species.";
RL Submitted (JUL-2014) 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:KFL44728.1}.
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DR EMBL; JPPQ01000083; KFL44728.1; -; Genomic_DNA.
DR PATRIC; fig|1522072.3.peg.4203; -.
DR eggNOG; COG4191; Bacteria.
DR Proteomes; UP000029094; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.250.2580; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
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; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFL44728.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KFL44728.1}.
FT DOMAIN 261..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 408..623
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 131..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68844 MW; B364903435829A13 CRC64;
MRRFIRNVRI FDGQGTAPFA GAVLIEQDRI AAVLRDEAMI AATTADQVID GQGGTLMPGM
VDSHTHLTWG SSVEKIYHQF ILPADELKVA AWRNARVLLD HGFTSAYSAG ALGDHIEPEL
ARAIAAGETP GPRLVPSTLE RSPEGEEGVE TGDVFNGRGA QSMRDFVAYC AQEGVQSLKL
VISGEDALKP GSSGDXXXXL AAALHEGTLE REAWRVCENG AEYLARLTIS ALFEGDAHRG
FACISRDVTD EAAVRASIET REQHLQSILA TVPDAMIIID ETGDITSFSA AAQRLFGYSE
TELVGRNVSC LMPQPDRDRH DEYIAHYLQT GERRIIGLGR IVVGQRRDGS TFPMQLSVGE
AGEDGQRLFT GFIRDLTAKE QDELRLKELQ AELVHVSRLS AMGTMASTLA HELNQPLAAV
ALYLETIRDM LDERDDEPFV SLRSVMDDAA QETLRAGHIV RRLRDFVARG EVDKSLHDLP
QVVAEASELA LVGARERGIR SFFAVDPAAT PVLVDRVQIQ QVLVNLMRNA IEAMAACPVR
DLKVATRLRP DGLIEVTVED TGPGIADEVR EQLFTAFKST KADGMGLGLS ICRTIIEAHG
GRIWMERPDR GGARFHFTLI HARAEEEHGG
//
