ID D8GUU9_CLOLD Unreviewed; 911 AA.
AC D8GUU9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kdpD {ECO:0000313|EMBL:ADK16976.1};
GN OrderedLocusNames=CLJU_c39520 {ECO:0000313|EMBL:ADK16976.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK16976.1, ECO:0000313|Proteomes:UP000001656};
RN [1] {ECO:0000313|EMBL:ADK16976.1, ECO:0000313|Proteomes:UP000001656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC
RC {ECO:0000313|Proteomes:UP000001656};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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; CP001666; ADK16976.1; -; Genomic_DNA.
DR AlphaFoldDB; D8GUU9; -.
DR STRING; 748727.CLJU_c39520; -.
DR KEGG; clj:CLJU_c39520; -.
DR PATRIC; fig|748727.19.peg.1209; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_0_9; -.
DR Proteomes; UP000001656; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
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; 3.30.450.40; -; 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; IPR029016; GAF-like_dom_sf.
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 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 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; SSF55781; GAF domain-like; 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 Ion channel {ECO:0000313|EMBL:ADK16976.1};
KW Ion transport {ECO:0000313|EMBL:ADK16976.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADK16976.1};
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}; Transport {ECO:0000313|EMBL:ADK16976.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 411..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 687..904
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 911 AA; 103436 MW; 330237BF54A53FFB CRC64;
MEVIIIDYNE RPDPYRILNK VEKEDSESER GKLKIFFGYA AGVGKTYSML REAHDIKNLG
KDIVIGYIES HERLETMDLT KGIESINTKV IDYRGVILKE FDLDAALLRK PEIILVDELA
HTNAKGKRHR KRWQDIEELL EAGIDVYTTL NVQHIESLND VVESITHISV RETIPDKVFD
NADKVEIIDI EPDELLKRFS DGKVYARDQV KSAFHNFFTK SNLYALREIA LRKTADRVNY
EIETARLSKG QITVVPASDQ ILACISSSPS SLRVIRTAAR MAEVYHSKWI VVYVETTKSQ
KLSKEDRKRL NSYFNLGEQL GGEVVTIYGD DIADQVIQYA KFRNITKIII GKNNKKTSKV
FHFYAKDVVD KLMDSNSYID VYVIPNSLYD RKSNKITKKF SKEFNLSLKE AIKAALILSI
VTCAAIIFDY VGFSEANVIM IFILGVIIVY MQTTGYLMGI ISSLVGVSIF NYLFVPPKRS
FHFYDKNYLI TFIMILIEAF VIGNLTNKIQ QDADESYTRE KRTQTLYRVT SKLLSAVGNS
DVVSIAIKYL SRLVDRTVVC YLSIDNKLST PFVYYLDELK KDDLILNKDE AAVAYWSFLK
GREAGSGTDT FYGARGYYIP VKVQNKILGV IGVSCEKDFL SHDQKFIVET VTGQMAIALD
REILVGQQEK SKVEIERERL RSNLLRSISH DLRSPLAGIK GAVSTIIENG KFIPEKTKED
LLNGIYDDTE WLISLVENLL SMTKFDEGNM KINKNLELVE EVVSEAVQRS SKYFKDHKIK
VEVPKKLIMV PMDGNLIEQV LINLIQNAAK FSKKQSFIQI KVYESVDDVF FEVIDDGIGI
SDKILPHIFD RFFTNGSSIA DSRRGVGLGL TICKSIVEAH CGTIEAENKK EGGAIFRFNI
PKGESTSNEL M
//
