ID A0A1I6DBH2_9PSEU Unreviewed; 856 AA.
AC A0A1I6DBH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488564_102176 {ECO:0000313|EMBL:SFR02779.1};
OS Lentzea waywayandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=84724 {ECO:0000313|EMBL:SFR02779.1, ECO:0000313|Proteomes:UP000198583};
RN [1] {ECO:0000313|EMBL:SFR02779.1, ECO:0000313|Proteomes:UP000198583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44232 {ECO:0000313|EMBL:SFR02779.1,
RC ECO:0000313|Proteomes:UP000198583};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOYL01000002; SFR02779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6DBH2; -.
DR STRING; 84724.SAMN04488564_102176; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000198583; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFR02779.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 623..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 856 AA; 93056 MW; 01FBECA3056EF72C CRC64;
MPSTQPERRR GELRIYLGAA PGVGKTFAML GEAHRRRERG TDVVVGLVET HGREKTQHLL
DGLDILPRRE FQHRGVDFTE MDVDALLARA PEVAVVDELA HTNVPGSRNE KRWQDVEELL
EAGIDVLSTV NVQHLESLND VVQRITGVQQ RETVPDEVVR RADQVELVDI TPEALRRRLA
HGNIYAAHKV DAALGNYFRV GNLTALRELA LLWVADQVDV ALQRYRHEQR ITDTWEARER
VVVSITGGPE SETLIRRARR IALRAGAELL VVHVMRGDGL TGATPELIAK CRKVAEGLDA
TFHQVVGDDV PTALLEFARG VNATQLVLGT SRRSRLARAL DEGIGAAVIH DSGPIDVHMV
THDEARRGLR WKIGVNALSR TRQLTGWLAS VLLPGLTAVL GLFWRDDITY STDLVGFLLA
TCVVALLGGL GPALFSAFLG AGLLNFFFTE PYYSLAVNSP ENVITLAAMV MVATIVALVV
DRAARLAEQG ARARTEAALL ASYSRTVLTS PYPLARLLDK IRENFGLESV ALLEKRGSDW
ERVACVGARP CDDPDEADAD IAVTTDIHLA LRGRTLPASD QRVLEAAAGQ ALMALRQQRM
ADETRVAQRK VETTELRTAL LSAVGHDLRT PLTSIKAAIG SLRDRELVLS EEDTVELMET
VEESADRLNG LVDNLLDSSR LATGSVAPVI RPVGYYEVVA RALSAVDERS TVSVSVDEHL
PPVSADIGLL ERVVANVIDN ALRHGRMSPR RPVDVDGDGQ VAQDEPEIAV RASAHGDQVE
LRVVDHGPGL HKKAVQGVFT PFQRLGDRDA TPGVGLGLSV AKGFTEAMGG EITAEDTPGG
GLTVVISLPV YEENRV
//
