ID G8TN28_NIAKG Unreviewed; 1441 AA.
AC G8TN28;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Niako_1342 {ECO:0000313|EMBL:AEV97713.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV97713.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV97713.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) 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};
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DR EMBL; CP003178; AEV97713.1; -; Genomic_DNA.
DR STRING; 700598.Niako_1342; -.
DR KEGG; nko:Niako_1342; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2207; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 1489484at2; -.
DR Proteomes; UP000005438; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 6.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEV97713.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AEV97713.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 880..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 927..1146
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1191..1306
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1341..1440
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1239
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1441 AA; 163159 MW; 3E6E6C6EE0E708EE CRC64;
MNLGDIYRGI AGKRLLYVLF FCLFAEILHA QPKYKIEHYA TEQGLSHRRV NCMMKDQEGF
MWFGTWDGIN RFDGRTFVSF KSSPEEKYQL GNSRIARIVE DQNGHLWVQA YDYQVYRFDK
KTEQFLPLST LLKSDHKIEF NNILQAADGY VWLQTKNDGI FRVSQASRPS IFHESISNPS
LISRLSRSSY AYLSQLSRFR LSGDDLTAIE EDTDHVFFGL SDGQLITFEK RSKSFTQRKV
ATGRINALLR SAKSDVLYAS TSLGEIVMIS LGDQRIATAN YATKESLSTL YEDKTGGLWI
EPEKMGALRF DPSTRSFQLF SVNTGTILSD NNNRYFWVLE DYKGTVWVSM KGRGFGYYKP
GSKSLENNLQ TPEGANYQLP ANIIGHYYDS AGILWLTTKE GGLVKIIIQD NDFEQQHLVD
QESARSGNEV RVMYNDQQGR LWLGTKMSGV SVFKNNIPIK GLFENEPAGG VVGVYAILQD
SKGNIWLGTK GNGLYKATPV NNEQTKYRLS HFQRHKEITD SLPFNQIYAL LEDKQDRIWV
GSLDNGLALI EQNPGGTRCI HSGNAFQNYP KGAFQNIRTM CLDAAGNIWL GTTTGLLVLD
ANDQHSAVYK YKTYSTIPGN KESLGNNDIL FVYRDRKNRM WLATSGGGFC EVIGDKPFET
LRFRNYTTKD GLPNDYILSC AEDSEGNLWL ATENGLSKFN PETRVFRNFD SYDALPPKIT
FSEASVTKAP ANKQLIFGTV TGYLSFNPDQ INTSRIKANI AFTGLQINNE DAGPKANTQL
LATDINYVSQ INLQYNQDII SIYYALLDPR GSGDRQGFAY RLLGFDSTWH NDWQVRKATY
TNLPPGNYVF EVKSLSHDLY SNQPYKQLAI TIMPPPWKTW WAYLLYALVI GVILFFIRRY
TLAMIRLRHK IAVEQKLAAL KMHFFTNVSH ELRTPLTLIV NPLEQVAKKG ELSPEMSGYI
DVARKNASRM VRFINQLLDL RKVQSEKASL RISRLEVVTF VKKITGHFTE AARSKRIHLE
VVPDQKECIA WVDAEKLDVV IYNLVGNAIK FTPEDKSIKI FIKSNPATQS FTIAVHDQGP
GVPNNKLEQI FDLFQEGEHT NGRELKGTGI GLALSREFVA LHGGAIWAEN NAEGGLTVTV
QLQSGAEYYK QQEASFVEQP QTTPVIGKPI EQQLLSQIAG NGSSQNPEAP LVLLVEDNDE
LRNFIKTQLG EHYRVKTARD GEEGLQKALE LIPDLIVSDI MMPKMDGLQM LDRVKNDVNT
SHIPVVLLSA KYSIESQIEG LRYGADHYIT KPFNNEFLIA SIDNLLQQRK KLFEALVEKK
KAVDLSPEPV VITSKDETFL KDVIRVVESK MEDPDFNIDS VAETMALSRT NFYKKFKSLT
TLTPMEFVRD MRLQRAKQYL DAGGHNISEV AYLTGFSNPK YFSTVFKEKY HVSPSDYIKS
K
//
