ID A0A0T5ZK46_9CHLR Unreviewed; 867 AA.
AC A0A0T5ZK46;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=XU10_C0016G0046 {ECO:0000313|EMBL:KRT63054.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63054.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT63054.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63054.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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:KRT63054.1}.
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DR EMBL; LDXM01000016; KRT63054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZK46; -.
DR STRING; 1640513.XU10_C0016G0046; -.
DR Proteomes; UP000051896; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 19..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..416
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 423..475
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 483..521
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 554..607
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 643..860
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 609..636
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 867 AA; 92527 MW; 38E0BA084B941F05 CRC64;
MPPTDPAPAR GDRLRRQGWA WYLVPAFLVV AAGAGLPRDG AWVATYLAGH ALAIAAVLAA
MLIHRPVPER PWRLLVLGLS VHFLGDVIGL PALAGLIPPL PYPSLADLLY LAGYGLIVAA
MVAAAAARGA LRQRGDLLDA AVLTLGLAIL SYAVIIGPHV GADPDLTLAG RIVSIAHPLI
DLALASVAAI LLMGGLRPSP AAVLFGIYIV AHLVADTIYE LEQASGTFVP SSVVTVLWPV
SLAVLGAASL HPSMTSLAAT EPEAFLPERW RVPIIGLAVL TIPVGLLIAT ATNPMGAAPI
AVMSAVLFIV ALVRLRGMAI DVEVSRRLVG ELAGARARYR DLVERVPAIV FTDRIGPGGT
SITEEYLSPQ ANEILGFEPD EVLADQHVWG AIIHPEDRER VATGYRDWVQ AILSDPAIAS
TTHSDEYRVV ASDDRVLWFR EVARAVAGDD GRHDHVQGII LDITEQKAIQ ARIHALALRN
ELLLESVGEG IYGIDLEGRA TFVNRAAAAI LGYDPSDLVG QPMHPRIHDR RADGSPYPVE
ACPIYAALRD GSVHAVQDEV VWRKDGSSLD VEYTSTPVRD EGGSIAGAVV VFRDVTARKW
ADEAIQAAYA DLENRVAERT QELEAARVEA ERANRAKGEF LSSMSHDLRT PLNAILGFGQ
LLELSTLAER DRESLEQILR AGRQLLAMID DVLEFTRVDS GRLTLAIEPI VVTEAVHEAM
DLVRTQAVER GVQLEWPSGA DPGLAVLADR RRLVQVLLNL LVNAVKFSRE GGTVTVAAEP
LAEGRVRIIV RDTGIGISPE RIPRIFEPVE VDSGGRSGSR SIGLGLVTGS RLVRAMGGSI
SVESQIGTGS AFSLDLPRAG SMPGPST
//
