ID J2CZ31_9SPHN Unreviewed; 620 AA.
AC J2CZ31;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI04_02409 {ECO:0000313|EMBL:EJK82504.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK82504.1};
RN [1] {ECO:0000313|EMBL:EJK82504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK82504.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK82504.1}.
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DR EMBL; AJVL01000058; EJK82504.1; -; Genomic_DNA.
DR RefSeq; WP_007710225.1; NZ_CP124576.1.
DR AlphaFoldDB; J2CZ31; -.
DR STRING; 1144307.PMI04_02409; -.
DR PATRIC; fig|1144307.3.peg.2173; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR OrthoDB; 9796100at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd19410; HK9-like_sensor; 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 InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EJK82504.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EJK82504.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..476
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 500..615
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 198..242
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 550
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 620 AA; 67923 MW; 305785EB92914B0D CRC64;
MPAIRPERSI VILLLALIIV VIAVSGTFWL YRSQQTGIGW VNHTLRVENR LSVILSRVQA
AESSQRGYML TRQEPFLAPF EDFKAGWRGE IASLRVDVRD NPVQVQAVDA LGAMLDRRLT
LMQGGVDLRR RGGAVDPNAF APGLAAMAQI RAQIEQMKLR EELLLRVRSI EASRLNIWVT
ASLAVSAAFV IILGMLALRT ARRRMEEALE SERALSEANA RLVAEAQERQ AVEAQVRQLQ
KMESIGQLTG GIAHDFNNML AIVIGSLDMV RRRLTPDTDA RVARGIDNAT EGAQRAAQLT
SRLLAFSRQQ PLDPQPTDVN KLVGGMSEML RRTIGETVRV ETVLAGGLWR ASIDSGQLES
AILNLCVNAR DAMPGGGRLT VETGNAHLDD AYATAHAEVL AGQYVMVSVT DSGTGMPAEV
VERAFDPFFT TKGVGKGTGL GLSQVFGFVK QSRGHVKIYS EPGQGTVIKI YLPRHYGADM
MDAPARTAPV ELPRARGEEI ILVVEDEERV RHMSVDSLRE LGYVIVQASD GEQALAMLAI
QPRIDLLFTD IVMPGINGRI LADRAREQRP DLKVLYTTGY TRNAIVHNGM LDPGVAFLAK
PFTFDQLAAK VRQVLDEGTI
//