ID D0LTT6_HALO1 Unreviewed; 2468 AA.
AC D0LTT6;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hoch_3278 {ECO:0000313|EMBL:ACY15780.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY15780.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY15780.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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DR EMBL; CP001804; ACY15780.1; -; Genomic_DNA.
DR RefSeq; WP_012828380.1; NC_013440.1.
DR STRING; 502025.Hoch_3278; -.
DR KEGG; hoh:Hoch_3278; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG1340; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000892_2_2_7; -.
DR OrthoDB; 9786165at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 6.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 8.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 8.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACY15780.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..200
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 219..493
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 1190..1261
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1265..1316
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1398..1451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1452..1523
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1591..1662
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1710..1762
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1783..1835
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1916..1968
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1969..2011
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 2044..2096
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 2107..2329
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2346..2463
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 646..733
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 2395
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2468 AA; 271386 MW; 8469F797E07DFEBC CRC64;
MNDSADGTES GRSPVLAVGV GASAESAQTF EELLRALPLD TGMALFLVQY MEPDDGAELH
TALAESTGHR VIAPEHGARV EANTVYLMQA GTELTIEGGR LDVGDPVLHR GMHRPINRLF
RSLARGFAGR AVGIVLSGVG RDGTAGLREI HAQGGLSIAQ EPETAAQGAM PRSAIDSGVV
DLVLPIAEMA GALEQFAATP YLRGAGDEVE DAAADPAGGA RTTMTLPPEV LEQVTEILGP
SLTMDVAHYK SATVERRTVR RMGLAGFQEI EPYLEHLRAN EEERELLVRD LLINVTRFFR
DGDAFELLSG VVIADIINSA GAQDTVRVWV PGCATGEEAY SIAIAFLDAM SSQSKRLTLQ
LFATDVDEEA LAVARAGLYG PEIADQVSEE HLERYFTRVN GRGYRVRPRL RDALSFAVHD
LCGDPPFSRM DLISCRNLLI YLRQQAQEDV LRALHFALEP TGYLFLGASE SVGALRELFT
TLSKPWRLFQ RAGAARPLLM RRGRSTGRLP RIAQRPPVDE VDIASAARDA MLAVRVPPSV
AVSHEGRVLY VHGDIGAYLH YPKGEPRLDL LADLRADLVT RVRAALYKCR RDGVTVEALS
TPERGGGPGT RITASPAPQL GEGAAVLSFE QVAGVEPADD TVPVETPEQE NLIEQLEREL
NATREDLRNT VEELESANEE LRTSHEESMS MNEELQSANE ELEAMTEELR SLNEELATIN
RQLKDKIGQL EKTHDDLSNF FASTKLATLF LDDERRIKRF TPAAAEFLQL DEEDEGRRID
DIARPLLHMD LDDDVAAVLD ELIPRTRELQ TPDGRWFVRR VLPYRTEARR IEGVVATWTD
ITELKRTAAQ LEVRERMQGV IARLGFKALG EDQDVLLAQV VREVQQTLAT DLCGILTLDS
EHSELMLEVG VGWNQGAVQS SRVPLGMDSQ AGYTLAAGEP VAVENLAEER RFKGSALMRE
HDVVSGVSCA IQDGDAAYGV LCAHTREPRA FENDEVHFLQ SVASLLAVAI SHRQTRQRLA
IERGVGQALA QSTSLDEAMP QIVGVFTREL DMDGGELWMV DEDGATLARR AFVMPEPYRS
SEAAARREGS LIRRGVGLVG RVWERGHAEW LSVLSEEQTL GGDELHELMG LRCGCALPIL
LGTEVIGAVS LFTRRRRLVD RQLVHSLDAI GTTIGEFVRR SEAESATRLS EMRLRMAIDA
AAAVVFESDV GARQVRSLFG SEALLGEVVE APLSLDTWME RVHPDDVARL EQELSEIVHG
TRQLQVLEYR LRHRDGRYLH VEVHARDTVG ADGVTRRNGV ILNVHARKQA EAELADRERR
MRLAVGALDA GVFAHAEPVG EELYLSARWL GMLGLAPSAL PPAPRFYDWL QAELIHEDDV
ASFANARAAF VAGHTGKLDL ELRLRHAEGH WMWGRMVADA VARDDEGRLL RLTGLLWDVT
AAKEAERRLR ESEENFRRLA ESIPHMVWTA RPSGGLDYCN QRALELLGRS QAELSQPDAW
LEAIHPSERA AVTAAWHEAM SLGREFRADL RLRDASCGAY RWHSVHAVPA HGDGDRDAPA
GERTGARVLR WFGTFTNIHE RKAFEDRLSE SEQRLQRTFE GSPLGIVFLQ RDGRMKRLNP
ALMRLLGLSD EDVARGLTWL DLIPAERASL YDEAMAQLER TGRVGPAERV LVAKSGRHIP
ALSSSFQIGQ GDEFVTFIVD LTEQKQAAAE RAKLAAIVES SDDAILSQSL DGRIESWNRG
AERLYGYAAD EAIGRPVEIL IPATHGDEND RLLAGVSAGD TVVQHETMRL RKSGAEVPVS
ITMSAIIDEM GACVGISMVT RDITEQKRAE ARLRESEDRY RENAAEMEAV YATLPVGLGL
SDRQHTFLRA NERLLELLEL ESARVCDSAI ETLLPALAVH VAPLIDQIFE SGEPILNREF
RAASGGGVER HWLSSFAPVF DTDEQVRAVS WMVQDVTERT EAETRLRESE WRFRQVLVNS
PLPMMMYDDA GRVLALSEAW TATTGYQLDD MPSIGRWAEL AYRDEAGDVL TYLGSLWSSE
ASGEHIELRV FAKDGEERTI LFSGAPLGTS PDGRRLRLWA GTDLTERKQA EEALREASAQ
KDQFLAMLGH ELRNPLAAIR GAAELLLLSD GGGDELERTR GIIERQSAHM AKLIDGLLDV
SRVVLGKIVL DSKVVDVVEI LRDLMQDHAD RIERSGLSLR LDLPGEPIWI DGDRVRLTQI
FGNLLANALQ FTSAPGTITI SAETIGSSPA GTALVRVRDT GAGIAPELLP HVFEPFRQAA
QNIDRAAGGL GLGLALVRGL VELHGGHIEA SSGGAERGAQ FTLHLPLAQR AREPVREEPA
LLGPRRLLVV EDNPDMAELL RDMLTRSGHQ VAVAHNGMQA LDVARKVEPD FILCDIGLPG
GMSGYDLARA IRKDDKLGDV QLVALTGYGR PEDRAEAEAV GFDTHLTKPV SMSAIQELLA
RGTGRHRA
//
