ID A0A154R4H2_9GAMM Unreviewed; 1175 AA.
AC A0A154R4H2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RhoFW510R10_10040 {ECO:0000313|EMBL:KZC33061.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC33061.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC33061.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC33061.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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:KZC33061.1}.
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DR EMBL; LVJU01000015; KZC33061.1; -; Genomic_DNA.
DR RefSeq; WP_068090260.1; NZ_LVJU01000015.1.
DR AlphaFoldDB; A0A154R4H2; -.
DR OrthoDB; 176203at2; -.
DR Proteomes; UP000076310; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF07494; Reg_prop; 3.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KZC33061.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KZC33061.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1175
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012859388"
FT TRANSMEM 765..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 819..1033
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1049..1166
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1098
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1175 AA; 127953 MW; 570E902EF77A746C CRC64;
MVLGVFVSAP GHAFAAPAAS GARAAGPLPT PQFRRYQTAD GLPGSTVYSV VQDKQGLMWF
GVGVDLVRYD GVDFQTFSHH SDDPASLPEG SVYSLFADRD NQLWVGGFGS GLNRHERESG
GFRHWRHDPV DPRSLASDNV WSITQTPDGG LWVATDAGLD RLLPDGRHFE HVRNPLGKNP
DEGFGAVRAL LAEPDGKLWI GSSLGVFVRE VDGSMRQVPI DPRLQALKVW RIQGGGDDVR
IAVRGGLLRV GADGKAWMYA PGQIPSIDVY SSTVDQAGHL WITTRNGLYL DDGSSQIHAI
SGQPLLLGSL PAQQVWQSLC DSEGGLWFVM GDGGIAYLAP GWNQFTRFTH VPDDSHSLRG
NAATAVLASF DGRLWVGGHG LVDKLDPITG DVQHAISGLQ GNVLDMAEDA RRRLWIVSEG
GVYRYADGKL VEVDLAASRV AHPRRLTMGP DRQIYLVSIR DGLFRIDPDT LAVDTKPVAS
ADDTGFVGNR LTPYNSLGWY ADQGRLFRWN AVRNELEPIA GLSDEGYIYA LEFTMDGFWA
ARNKMFEHYR LDAGKVVRDQ LVPIPSSWPS MVLIAMHVDR QGRFWMFCKN GLWRFDPHSG
ELKSFGLRNG LVNGEVRGDS PAVTPDGTIY VASLGGVFGF QPDRAPATAR PAGVVITGAS
VRHAGAVREL PVRAGSVQLA WSDRGLRVEV RLSSFVDPAS NRYRFRLHGF DTAWVNTGNH
GERDFTGLGA GNYTLEVMAA GADGMWVKLA RPLSIHVDSP PWLRWWAWAI YVLLLAVLVG
LVLRSWRRRL AQRHHMQLVE QQRQLAEAAS AAKTQFLATL SHEIRTPMTG VMGMAELLLS
TPLDPQQHDY TKAMQRSGGM LLKLLNDALD LARIEAGKLE LEPAPFEPRQ LLEDVVQLEQ
GLAHAKGIRF VLEMAEDLPA QLLGDALRIK QILLNLASNA LKFTEHGKVT LRAQRTDEGL
LLSVSDTGPG IPEASQARLF QRFEQAEGPQ RRVGSGLGLA ICRELVEMMG GSIELESRLA
HGSTFRVRLP LAVPASTAPV AWAPGRPCQL LLVEDDTIVA TVIRGLLERE GHTVVHVVNG
LAALAELAHA GFDAVLLDLD LPGVDGFQVA RLIRQREHAG QHLPIVAVTA RSGSEDEAKA
RAAGMDGFLR KPVSGERLAD ALARVLGGAD APLPA
//
