ID A0A2D2MA47_9PSED Unreviewed; 921 AA.
AC A0A2D2MA47;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CS390_18580 {ECO:0000313|EMBL:ATR84389.1};
OS Pseudomonas sp. HLS-6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2049589 {ECO:0000313|EMBL:ATR84389.1, ECO:0000313|Proteomes:UP000230810};
RN [1] {ECO:0000313|EMBL:ATR84389.1, ECO:0000313|Proteomes:UP000230810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLS-6 {ECO:0000313|EMBL:ATR84389.1,
RC ECO:0000313|Proteomes:UP000230810};
RA Hu Y., Zhang T., Lei D., Yao S., Lin K., Chen X., Cui C.;
RT "Complete genome of Pseudomonas sp. HSL-6, a multiple-antibiotic-resistant
RT bacteria isolated from drinking water source in East China.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP024478; ATR84389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D2MA47; -.
DR Proteomes; UP000230810; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ATR84389.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000230810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..244
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 672..791
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 828..921
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 225..256
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 721
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 867
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 921 AA; 100971 MW; 34AF728A008D619B CRC64;
MLNRLGIRSR VLLLALLPTS LMALVLGGYF TWLQQNELQS QLLQRGKMIA EQLAPLVAPA
LVSNNPAQLE RIAAQALEQA DVRAVGFLAP DRSSLAHAGP SMLNQAPNGD TTQLLQRSGS
DATRYLLPVF GRHRDLAGEL IPGESHRLLG WVEVELSHDG TLLRGYRSLF ASMLLIFIGL
VVTALVALRI SRTINGPLGQ IKHAVNQLKD GNLEQRLPTL GSYELDELAD GINRMAQTLQ
NAHEELQHSI DQATEDVRQN LETIEIQNIE LDMARKEALE ASRIKSEFLA NMSHEIRTPL
NGILGFTHLL QKSELSPRQL EYLGTIEKSA DNLLGIINEI LDFSKIEAGK LVLDSIPFNL
RDVIQETLTI LAPSAHAKQL ELVSVIYRDT PLSLVGDPLR LKQIITNLVS NAIKFTREGT
IVARVMLEDD DDDQEDSVHL RISVQDTGIG LSPQDVRALF QAFSQADNSL SRQPGGTGLG
LVISKRLIEQ MGGEIGVDST PGEGSQFWVS LRLPKALDDA EDLPPSSLQG RRTAIIDPHP
LACQALQHQL QDCGLSITVF NTLDQLLNGM DAARLAGQPF ELAVLGVSLA NLSPERLGQH
VQTLEKQGCQ TMVLCPTTEQ RAFQACLPNP HSQLQVKPTC TRKLRRALLD LTEPRRSEEE
LTRQVPGQRQ PKVLCVDDNP ANLLLVQTLL EDLGASVEAV DSGSAAIKAV QEDCFDLVLM
DVQMPGMDGR ECTEQIRLWE TANDSAALPI VALTAHAMAN EKLALLHSGM DDYLTKPVSE
RQLAQVLLKW TGLSLAKPPV ERFSERPVDS AELKVLDPEE GLRLAAGKPD LAADMLAMLL
ASLDADRDAI RTARHASDRT ALIERVHRLN GATRYCGVPQ LRAACQRCET LLKQNAPQAQ
QALDELDRAL ARLSAQARLS V
//