GenomeNet

Database: UniProt
Entry: A9WGU0_CHLAA
LinkDB: A9WGU0_CHLAA
Original site: A9WGU0_CHLAA 
ID   A9WGU0_CHLAA            Unreviewed;       952 AA.
AC   A9WGU0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Caur_3057 {ECO:0000313|EMBL:ABY36256.1};
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36256.1, ECO:0000313|Proteomes:UP000002008};
RN   [1] {ECO:0000313|Proteomes:UP000002008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC   {ECO:0000313|Proteomes:UP000002008};
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CP000909; ABY36256.1; -; Genomic_DNA.
DR   RefSeq; WP_012258909.1; NC_010175.1.
DR   RefSeq; YP_001636645.1; NC_010175.1.
DR   AlphaFoldDB; A9WGU0; -.
DR   STRING; 324602.Caur_3057; -.
DR   EnsemblBacteria; ABY36256; ABY36256; Caur_3057.
DR   KEGG; cau:Caur_3057; -.
DR   PATRIC; fig|324602.8.peg.3460; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_15_0; -.
DR   InParanoid; A9WGU0; -.
DR   Proteomes; UP000002008; Chromosome.
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; cd00130; PAS; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          220..289
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          294..344
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          345..416
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          426..477
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          495..714
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          741..861
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         790
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   952 AA;  106311 MW;  599560545A07198F CRC64;
     MSVDLLTLSI ALNLANLLQS AALTGLALAN RDRVGPVWWA AGMGVLAAGL ILTTLRDVAL
     LALELHAISN ALVGIGMLLL HYGVCRFFGD SGGRRWFWLA GGLIVAANLM LVFTGDAPPL
     RRILFSVVVA LVSMLIAQRL LRELRTDTRP VVLFLAIVFL VNSTFFALRA VASVAESDWL
     TVSPPWQTAT YLVAIATTTL WTFGLILLVN QELVNRQHEA VQQLEQIFAA QPDAVLLSRL
     TDGVFVKVNH GFTTISGYSA DEAIGKDALT LNLWRSPEDR RRWAEIMRRE GACSGMEFDF
     RRRDGTFRTC ILSSQVVMIR GVPHAISIVH DISERKRMEE ALRRSDARYR LIAENTTDVI
     WLYDPFKSQF TFFSPSIEKL IGYSAAEALD LPLSAFLKPD SIQHVKTALD YMLHEWEGEL
     TNAPPWTAEI DLIHRDGQIV QAEIVTSFVR DEEGQLMVLG VARDITARKQ TEIELRLARQ
     QAEAANRAKS AFLANVSHEL RTPLHAVLGF AQLMSRDDNL TATQHEYLAI INRNSEHLLH
     LINEVLDLAK IESGRYTYTP NPLDVRRLLA DLQALFGPQA EAKQLQLIVT CEEQVPPMIV
     SDEAKIRHIL INLLGNAIKF THGGSVRLRA DTDKQQMYFI VEDTGVGISP LEQPYLFRPF
     FQGKQTANAS SDTGVGLGLS ISYEFARLIG GDLSVYSAGE GQGARFTLTL PLRTPVTSSF
     VLPAEPVKRA IQVRADQPVY RMLVADDQPT HALLLISLLR RLGFAVQSVT DGEQALAVWR
     EWQPHMIWLD LRMPQMDGLT VARQIRAICA TEPGLLQPVI IALSAHVLGD TAASVLAAGC
     DEFLAKPFPE HEVVRLIEQH LNVQFEYASV VIREVPETAI HDQGYHPAWC QALRQAVQVA
     HFQRLQELVG MIEDQRPDDA RQLRNWIETF DYEAVRQWLD RLVSSQTVDR VV
//
DBGET integrated database retrieval system