ID D0LRA2_HALO1 Unreviewed; 1453 AA.
AC D0LRA2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hoch_4639 {ECO:0000313|EMBL:ACY17130.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17130.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY17130.1, 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};
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DR EMBL; CP001804; ACY17130.1; -; Genomic_DNA.
DR RefSeq; WP_012829728.1; NC_013440.1.
DR STRING; 502025.Hoch_4639; -.
DR KEGG; hoh:Hoch_4639; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR eggNOG; COG2201; Bacteria.
DR eggNOG; COG5002; 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: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:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17580; REC_2_DhkD-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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; 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; 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; 2.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
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; 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); 3.
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; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000313|EMBL:ACY17130.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Transferase {ECO:0000313|EMBL:ACY17130.1}.
FT DOMAIN 12..202
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 224..478
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 833..903
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 906..959
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 960..1030
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1031..1083
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1094..1314
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1336..1452
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 485..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 639..701
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 489..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 25
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1385
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1453 AA; 162122 MW; 56FCDB9BA75B1C6D CRC64;
MADIINDESV QPSQRPSHVV GIGASAGGLE PLQQFFEHLP AKSGMAFVVV QHLSPNYKSF
MAELLAKQTV LPIESTKDGA PLLPDHVYLL PPNKSMQVKN WVLQVEPRDL SARPPKPIDT
FLHSLAEDAG RRAIAVILSG SGSDGARGAL SVHHAGGLVI AQSETTAAFD SMPRSAIEIG
AVDLTLAPDQ IPLAVANHAG IAVDATRLPA PVPLLDATSQ IFALLRERHQ VDFTHYKTTT
IWRRINRRLQ FKSMSLDDYM TELSENSAEL DKLYRDLLVE VTSFFRDPGV FAELRACIDR
LIAELPENEE FRAWVAGCAT GQEAYTVAIL VREAFRAAGR PVSAKIFATD VHTTSLDQAS
VGIYTEDNLQ SLPEQFRHDY FVQRDDHYQV SNDLRSILVF APHNVIRDAP FTRLHLVSCR
NLLIYLQPVA QKKALSLLHF GLRVGGVLLL GPSESPGEFT DCFDVVSENS RIYFKNKEKR
LMASLPAAPQ SPRLSSNTRP LNSRHETRLQ RARELLLERS PPAVLLDGHR DITHTLNGGS
HYLSQREGRA SLHILDLIHP DFKLSLPRLL DSVAETQESA SAAPIPFATD GETQRMVLSV
LPVTANEELN YLLIFETVVT NDVPVSRQPP GPEVQSERHQ WVERELEETK AKLQATIEQM
DANTEELQAT NEELTAANEE LQSTNEELHS LNEELFTVNS EHQAKIQELS ELTHDMDHLL
ESTEVHTIFL DRELRVRRFT PKVGDAFNFL PRDRGRSIED FTHNLGYKDI PVDLARVLET
GKSIDREVTG PEDKIYLLRL RPYCGDDQTI NGVVLTLIDI SELKHAEKDM RLSEQRYRAL
VRASADMLWI TNASGAFAEP QPEWERYTGQ SWESHQGFGW LQAIHPDDRD DIQGIWRHAV
AIGSVYSAEG RLWSVKHRQY RRFHVRAAPL RGDDGEIREW VGNVADVQAR WSAERELRRK
ETQLASIMRN ASAFIYLKDE KGRYLATNQR FATWLGRSSE EIHGCTDFDI FPTETAERMR
LGDKLAMSGE LFHEDEEIEY EGREVTWLTT KFPVKDEDGA TEGVAGISTD ITERTLAEGR
REIELERRDR FLAMLSHELR NPLAGITSAV GVLSLAGKEK LPPPALRAFE VLKRQTSHMA
HLLDDLLDVT RFVRDRLSLH RVLLDLREVV EAAVTLVTER AQTKNITLSL ELPPMPVPLH
GDALRLQQVI VNLLTNAVKF TPAGGRVGVV LVSTDSENVL TVEDSGVGMS DAELERAFEL
FYQGDESLDR PDSGMGVGLA LVRRLVLMHE GEVSAASPGP NQGCVFTVRL PRMTNAPTQT
SDSDGGSLQP PAARPRILII EDIEDTRAMV AEYLEALGYV VTQAADGNAG LAKLLEERPQ
VALIDLGLPG ISGFEVAKQV RDSPNLSETW LVAITGYGRH EDRQAALEAG FDEHLVKPVA
LQRLHKLIAA RIE
//
