ID A0A1V4LGY7_9PSED Unreviewed; 925 AA.
AC A0A1V4LGY7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BZ163_31945 {ECO:0000313|EMBL:OPK06304.1};
OS Pseudomonas sp. VI4.1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK06304.1, ECO:0000313|Proteomes:UP000189889};
RN [1] {ECO:0000313|EMBL:OPK06304.1, ECO:0000313|Proteomes:UP000189889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VI4.1 {ECO:0000313|EMBL:OPK06304.1,
RC ECO:0000313|Proteomes:UP000189889};
RA Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA Gawronski S., Vangronsveld J.;
RT "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT isolate from crude oil contaminated soil in Bobrka, Poland.";
RL Submitted (FEB-2017) 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:OPK06304.1}.
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DR EMBL; MULM01000184; OPK06304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4LGY7; -.
DR Proteomes; UP000189889; 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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OPK06304.1}; 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:OPK06304.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..925
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012415117"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 792..911
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 841
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 925 AA; 102040 MW; 08E4E2278D1BF7DA CRC64;
MRWLRIAIGF TVTLMTLLCM LPAQAAQGSG WAVLLDEQGD LQLSDIRSAR YTNQFSPIEL
DHLTAAEPDG AMWLRFRLAP GKHEQLLRVF APDLSDLDLY VLEGDSLIEE LDGGADQPRS
ERPLPNSDFM LPLPQSDKPL DVYLRLVSEH QMRPYITLQS AIMTAANQNQ TLIYGLLFGC
LGMLILHNLI RYAYTRSRSC LWLSGCEALL MLSLVLLLNL AGPWLPDWHA IQTPGAYLAL
LLTAPCGLMF AYRFFAPLGP HPLNKLLLGD IVVIIACGLL LLFVNTLPLN IITYALVALA
GLSMLFVSAH HWQKGYRPAR LFVAAMVVFN VGTLIILPAL LGLTLVEPQG LITALLVFIC
ISGLLMSIAL SERQRSITED RFSLSRDLAA SNAEINAKAE FLAKISHEIR TPMNGVLGMT
ELLLGTPLSV KQRDYVQTIH SAGNELLTLI NEILDISKLE SGQIELDDVQ FDLNALIEDC
LSIFRAKAEQ QNVELISFIQ PQVPRVISGD PTRLRQTLLS LLENALKKTD EGEILIVVAL
DERSAKPRLR IAVQDSGEPM DTEERDALMH AELHSKNFLS APRLGGNLGL VIARQLIRLM
HGEFGIKSGS TQGSTLWLTL PLDPDRLEHP TSDLDGPLQG ARVLVVDDND TCRKVLVQQC
TAWGLNVSAV PSGKEALALL RTKAHLRDYF DVVLLDQNMP GMTGMQLAAK IKEDPSLNHD
ILLIMLTGIS NAPSKIIARN SGIKRILTKP VAGYTLKTTL ADELNQRDKG LVASHQLPPG
PALPVKVPSD FRILVAEDNS ISTKVIRGML GKLNLQPDTA SNGEEALQAM KAQRYDLVLM
DCEMPILDGF SATQQLRAWE VGNQRTRTPV VALTAHILAE HKERARQAGM DGHMAKPVEL
SQLRELIEHW VAQRDEQNRA ATQTS
//
