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Database: UniProt
Entry: A6VCW2_PSEA7
LinkDB: A6VCW2_PSEA7
Original site: A6VCW2_PSEA7 
ID   A6VCW2_PSEA7            Unreviewed;       942 AA.
AC   A6VCW2;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 2.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=PSPA7_5576 {ECO:0000313|EMBL:ABR86205.2};
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR86205.2, ECO:0000313|Proteomes:UP000001582};
RN   [1] {ECO:0000313|EMBL:ABR86205.2, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86205.2,
RC   ECO:0000313|Proteomes:UP000001582};
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR86205.2, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86205.2,
RC   ECO:0000313|Proteomes:UP000001582};
RX   PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA   Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA   Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT   "Complete genome sequence of the multiresistant taxonomic outlier
RT   Pseudomonas aeruginosa PA7.";
RL   PLoS ONE 5:E8842-E8842(2010).
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};
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DR   EMBL; CP000744; ABR86205.2; -; Genomic_DNA.
DR   RefSeq; WP_033997462.1; NC_009656.1.
DR   AlphaFoldDB; A6VCW2; -.
DR   GeneID; 77223404; -.
DR   KEGG; pap:PSPA7_5576; -.
DR   HOGENOM; CLU_000445_105_0_6; -.
DR   Proteomes; UP000001582; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16938; HATPase_ETR2_ERS2-EIN4-like; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..942
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020036191"
FT   TRANSMEM        188..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          421..641
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          659..781
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          809..928
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         713
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         858
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   942 AA;  103821 MW;  420E5CB26745EFE8 CRC64;
     MVRLRIAIGL LVSCLLLLLG PISPAVADDS GVSSVPLQTT ATTPSANQNW RVLRDESAQL
     RIADVLQRKE QFRPLAKRSF IFPASTQAVW LQVQLPEQKA PSWLWIFAPR VQYLDYYLVQ
     DGQLVRDQHT GESRPFQERP LPSRSYLFSL PVDGKPMTLY VRMTSNHPLM AWFDQIDEAG
     LVGLEKPAYA FGMLLGGMLL LLMYNLIRFA YSRSASSLWL AAVHAALAVC AAANLGLVAF
     WLPGLRFNQS LTADLGALGA AVSLLWFACS FFRGTAESRL NRLLQGEALL ILAVGAIIAF
     TQQLWFSWLI YLLVILSSLS VPLVAAWHWY RGYQPARLIV AGMIVFNAGF MVFLPVLFGT
     RQLDPGWLVL GVFSFATLAG LVLSVSLTER QRLIQQLNLQ QRTSEAAHTA ELQTKAEFLA
     KISHEIRTPM NGVLGMTELL LGTPLSAKQR DYVQTIHSAG NELLTLINEI LDISKLESGQ
     IELDEVQFDL NALIEDCLDI FRVKAEQQRI ELISFTQPQV PRVIGGDPTR LRQVVLSLLD
     NAFKQTEEGE ILLVVALDEQ SGAPRLRIAV QDSGHPFDAK EREALLTAEL HSGDFLSASK
     LGSHLGLIIA RQLVRLMGGE FGIQSGSSQG TTLSLTLPLD PQQLENPTAD LDGPLQGARL
     LVVDDNETCR KVLLQQCSGW GLNVSAVSSG KEALAQLRTK AHLREYFDVV LLDQDMPGMT
     GMQLAAKIKE DPNLNHDILL IMLTGISNAP SKIIARNAGI KRILAKPVAG YTLKATLADE
     LAQRGVSGVT NYLHPAKEAQ APSLPSDFRI LVAEDNSIST KVIRGMLNKL NLQPDTASNG
     QEALAAMKAT QYDLVLMDCE MPVLDGFSAT EQLRAWEAHE QRPHTPVVAL TAHILSEHKE
     RARLVGMDGH MAKPVELSQL RELIAYWVGE RDRRRQGDAL PS
//
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