ID J3GSX9_9PSED Unreviewed; 794 AA.
AC J3GSX9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI29_00637 {ECO:0000313|EMBL:EJM74205.1};
OS Pseudomonas sp. GM49.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144331 {ECO:0000313|EMBL:EJM74205.1, ECO:0000313|Proteomes:UP000007288};
RN [1] {ECO:0000313|EMBL:EJM74205.1, ECO:0000313|Proteomes:UP000007288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM49 {ECO:0000313|EMBL:EJM74205.1,
RC ECO:0000313|Proteomes:UP000007288};
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:EJM74205.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKJL01000024; EJM74205.1; -; Genomic_DNA.
DR RefSeq; WP_007994002.1; NZ_AKJL01000024.1.
DR AlphaFoldDB; J3GSX9; -.
DR PATRIC; fig|1144331.3.peg.602; -.
DR Proteomes; UP000007288; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 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 Kinase {ECO:0000313|EMBL:EJM74205.1}; 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:EJM74205.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..794
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003767833"
FT TRANSMEM 182..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 424..645
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 670..783
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 719
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 794 AA; 88176 MW; 44FB4B240C16FA43 CRC64;
MRYLLMLLLC LPLLANAVEF DEYTQSLPLG RSLQVYEDAG GQATINDIRA QAAAGTFTPH
HKDTLNAGYS RSVFWLKIDL HYRPTNPAAQ RTWLLELAYP PLDHLDLYLP DAAGNYQLVR
QTGDALPFAS RQIRQNNYLF DLTFKPDQAE TVFLRLQSEG SIQAPVTLWS STAYLEEQPV
RLYVLGLIYG VLLGMLVYNL FIYLSVRDTS YLYYIFYIAS FGLYQLSVNG AAVQYFWPDN
PWWANAATPF FIGCAGLFGS QFARSFLQMA THSRWLDRLL LALVAFGALV VGLSLMTSYA
LALRLATALA LTFTVVIFAA GIFAWLRGLR VARYFIIAWS AFLLGGIVNT LMVLGYLPNV
FLTMYSSQIG SAIEVALLSL ALADRINDMR EQQAQTLFDA SQKLEVLNQQ LARSNKLKDE
FLATLTHELR TPMNGVIGSL ELMQTVEMDP ELEQYQQTAA GSARDMMRMV NGILTLTELQ
AGKLKASTDT FSLRGMVEAL RSQFEGNASS KSLDFKVDVA TGVPDRVHGD NVKIAQCLEC
LLDNAIKFTR VGGLALRVTG KALEPDRLAL TFAVIDTGIG FTDLGEATMY QRFFQLDGSM
TREYGGLGVG LAICRQLVEL LGGRLTHRTE PGRGSRFQLD VEVGLPVPER PVTPLMPRDF
PRLRLPQDCA VLLVDDNGIS QLVMRGMLLK LGFRVRTADS ADVALDLLQR EVFDAVLVDC
QLPLQDGESV CCQIRALPDY AELPLFMIAL GGDRERCPTG AVIDHLSKPV KFEDLQAALY
RRVLCPRQGE SADS
//
