ID U2HV22_9SPHI Unreviewed; 577 AA.
AC U2HV22;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M472_11415 {ECO:0000313|EMBL:ERJ59382.1};
OS Sphingobacterium paucimobilis HER1398.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ59382.1, ECO:0000313|Proteomes:UP000016584};
RN [1] {ECO:0000313|EMBL:ERJ59382.1, ECO:0000313|Proteomes:UP000016584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HER1398 {ECO:0000313|EMBL:ERJ59382.1,
RC ECO:0000313|Proteomes:UP000016584};
RX PubMed=23929486;
RA White R.A.III., Suttle C.A.;
RT "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT Member of the Genus Sphingobacterium (Bacteroidetes).";
RL Genome Announc. 1:e00598-13(2013).
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:ERJ59382.1}.
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DR EMBL; ATDL01000015; ERJ59382.1; -; Genomic_DNA.
DR AlphaFoldDB; U2HV22; -.
DR STRING; 1346330.M472_11415; -.
DR PATRIC; fig|1346330.5.peg.2725; -.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000016584; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; 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; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..220
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 229..273
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 362..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 577 AA; 64985 MW; 12AF822E50F96518 CRC64;
MKMNIKTKIT FGVGLLFFLI VLLAAVSGWY VNQLKRDTNN ILVANYNTLL YANNMLAVLD
ELDTDPVAVS LFKENLDKQL LNMTEVGEKE ATQLILEHLQ ALEKKPDDIL LLATIRTDIT
GLMRLNMEAI QRKSDVAGDT AHHAIVIISI TGGLCFLIAF VLLVNLPSSI ANPITELSES
IKEIANQNYK KRVFFSGHRE FGELADSFNT MAEKLEEYAD SKLDKLLKSK KRIETLIERM
HDPVIGTDEQ EYVLFANEQA CKVIGMKKEE LIGVSIRDLA LHNDLLRDVY RDWDKEQERS
GNNKVLKIYA DSKESYFEQE LVDIGIVPTG ESQEQFIGRV ILLKNVTAFK EMDLAKTNFI
GTVSHEFKTP IASIKLGVQL LENRQVGELN DEQTNLVSGI KDDLQRLLDI TGELLNMAQV
ESGAIQMNVA LAEVRPIVEY AVEANRVVME QRHIKMDVAI DPVVTTVRAD SEKTAWVLTN
LLSNALRYSH DESIVYIHVY SKEEKVWFSV RDTGQGILPE YMDKIFYRYF RVPGSKKEGT
GLGLSISKEF IEAQGGEIIV ASEYGVGSIF SFCLKIS
//
