ID A0A3E1RG19_9BURK Unreviewed; 1947 AA.
AC A0A3E1RG19;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DIC66_05615 {ECO:0000313|EMBL:RFO98191.1};
OS Rhodoferax lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO98191.1, ECO:0000313|Proteomes:UP000260665};
RN [1] {ECO:0000313|EMBL:RFO98191.1, ECO:0000313|Proteomes:UP000260665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO98191.1,
RC ECO:0000313|Proteomes:UP000260665};
RA Park M.;
RT "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT lake.";
RL Submitted (MAY-2018) 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFO98191.1}.
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DR EMBL; QFZK01000002; RFO98191.1; -; Genomic_DNA.
DR OrthoDB; 5519028at2; -.
DR Proteomes; UP000260665; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR036641; HPT_dom_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 6.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000260665};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 115..304
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 395..439
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 467..521
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 522..595
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 599..652
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 914..987
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 991..1044
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1045..1117
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1132..1184
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1202..1423
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1446..1571
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1592..1710
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1759..1860
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1501
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1643
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1798
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1947 AA; 214160 MW; DC059AF52E8995B3 CRC64;
MPAGLAEILF YACIPLAFAA VFVAAVWAPQ YIQRLAMARP AQRLVLYPVP MLIALLCLAA
GLAATVYFAD AARHAAYDDA RTHFLKVSDQ LESDVQTQFN DIERVLNGLR GLYESSDDVS
VREFRRFVES SDPHQVSPGF RGLGFIERVP RPELAAFVAN MRRNFLASYE ARTHGDKPDL
FLVKYLEPLS RNVEAIGYDI GSDPQRRAAA ESAMRSGQAT LTPRISLLQD SLKRPGFLLL
LPIYAGASEP DSQDSRVRDL LGWAFAPVVL SELMASGAGV DVRLVNYQLF DAPDLNAKSL
LYDSQLPAGE VNAPESLTRQ EHSAFSVVRA VLLGGQVLYL RTNSSPAFEQ DFHPREHLKA
AVLGSGLSVL GAMVLWLLMA GRARAVDLAQ SMTHDLERLA MVAKRTSNAV YFADTQWRIS
WVNEGFTRMS GFMPEEAIGM RPSQLLHSPL ADPQTPLIID SQAEAGGRVE IQVLQRSKAG
RDYYADLEVL PILDSKGRIT GYLSVQSDIT EVVQAKAALL LEKERAENIL TATNVGTWES
NMQTGEQRWN DRWSAMLGFS REEVVPGVDQ FWQQRVHPVD RERLKQAMAD CIAARTDSYA
CDVRALRKDG QWMWVLSRGK VMSRSPDGSA EWVGGIHTDI SESKQVELNL RDLEAFLDRA
GRIAGVGAWQ LDLKTRKLVF SAQTCAIHGL PADYEPTEKT ALDFYPEADR QRVVDAVKRA
EKDGTSWDLV VEFRNVQGEQ LWVRLFCEVG FDDSGPVRLM GAFQDVTKSY LSQLEVERSG
ALLRGAIEAI NEAFVLYDPQ DRLVLCNDKF RAINSRSSDL LTYGASFESI IRGGAERGQY
LEALGRVDEW VEQRMAAHRS GNVSMEQQLQ DGRWLKVIDQ RMPDGHTVGF RVDITELKLA
TAAAELTSAQ RGEEQKRMQS ILEGTQVGTW EWNVQTGHSL YNEQYVGMLG YTLQELEPLG
YDTFVRLVHP EDLAASAQKM QEHLRGESSG YEIEVRMHHK QGHWIWVLAK GKRAKGPDEG
QSEWVYGTHM DITERKRAEQ QLAQTMATLQ NVLDSATAVG VVTLGLDHTV RVFNKGAENL
LGYSAHELVG QQSADRFFEL SELGALRETL ELMLGHVPDL DEVFAHVVQT RDAQEWTLVR
KNGTRFKASL IFSPMRDVQG AQEGHLAVIY DISRQKEYES SLREAMRLAE QSSVAKSQFL
ANMSHEIRTP MNAILGMLQL LRNTALNAQQ GDYAEKAVGA ARSLLGLLND ILDFSKVEAG
KMQLNPEPFL LDGLLGDLSV ILSSNLGAKN VDLVFDVDSA IPRELIGDAM RLKQILINLG
GNAVKFTEKG EVVVRWTLLA RTPERVKLGV AVVDTGIGIA PENQSRIFDA FTQAEANTTR
RFGGTGLGLV ISTRLIRLMG GELQLSSVLG QGSTFSFTLE LQAADFQPAA PLLTVGPASR
TEAAVRVLLV DDNPQALATS AAMMRGLGWD VTLAASGAQA LDLLKADLAA QAAPWDALFV
DAEMPDMDGW DTLRNVCRLY ASRKPPLLIL LSRQSRGALS HRTEREQELL NGLMVKPLTA
AMFTRALEQA RNGSGLQPTQ PQVSPQRLHG MRVLLVEDNL INQQVAQELL SAQGARVTLA
DNGALGLDAI RSAQPPFDVV LMDLQMPVMD GLSATRLLRT DKRFAELPVI AMTANAMHSD
REDCLTAGMN DHVGKPFDLN QLVQTLITHT RWVERTGPVG GIVRRRAQPS VVQPALVDAV
QAGADGLEIG LALARMGGNR QLLQRAITGF VADARLLPER LDQCLHQGDL PALKRELHGF
KGLSATVGAP ALSAFAAEAE KHLQSPQGAL AWQARAPELT ALLGRYLPLL EDVAGQLGAN
AHGDSPAVGT VDTLELAPLR ELLVALQTSD MVALELYAAL RQKMGAGISQ AMEPLDLAMA
DLEFEAAATE CEKLLRNIDT RQGPVFS
//
