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Database: UniProt
Entry: A0A2D2MA47_9PSED
LinkDB: A0A2D2MA47_9PSED
Original site: A0A2D2MA47_9PSED 
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
//
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