ID Q47BP5_DECAR Unreviewed; 1560 AA.
AC Q47BP5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Daro_3006 {ECO:0000313|EMBL:AAZ47736.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ47736.1};
RN [1] {ECO:0000313|EMBL:AAZ47736.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ47736.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) 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}.
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DR EMBL; CP000089; AAZ47736.1; -; Genomic_DNA.
DR STRING; 159087.Daro_3006; -.
DR KEGG; dar:Daro_3006; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR HOGENOM; CLU_245954_0_0_4; -.
DR OrthoDB; 8552871at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd02205; CBS_pair_SF; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
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; 4.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; 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; 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:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF13185; GAF_2; 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; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
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); 4.
DR PROSITE; PS51371; CBS; 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..70
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 76..136
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 141..199
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 205..264
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 351..404
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 655..708
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 709..780
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 778..833
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 830..876
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 903..955
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 991..1212
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1234..1350
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1388..1482
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 250..277
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 946..984
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1465..1522
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1283
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1427
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1560 AA; 173241 MW; 61312E1A5C00B55C CRC64;
MHTMPSSTLG DIMTSDVRSL PPQATLEDAA KLMAAEHISS LLVIADGEAL GIVTESNILR
ALHARQPRET RLDVIMSQPL ITAPSDLNLI SARRLVEERN IRHLVVKNPN GTVAGIVSDT
DFRIRLGTAA FQHLRTLEGI MDRQIPKLPP DALLDQAIAC MVNNAADYLI VSNDDTPLGI
LTERDIPRLL DKFLTPHDVR LGETMSSPLR SVNVEMSVTG ALEAMNRFHL RHMVVLDNNG
KILGVVSQRR LFEQLALERL ENALHQMQQE RDRLRLEAHL QLALDVAGAG SWEYQHDTDR
HIVSDGVQAL LGCTQDDTPR TLNEWMERIH PDDRHLLATA ASADHGKTPS QVVEYRIRHQ
DGHWIWVENR SCVTERNADG SPMVTAGILN DITERELARQ QITRQNRALR MMTAVAQILV
RYTDEQQMLA EICTVAVEVG GYMMAWVGEA RTDEKKSIVP TAESGLIGDY LKQLNISWAD
APNGQGPTGR AIRTGVPSII RDTETDPSFT PWREAAKTLG FRSSIALPLR VDGRIVSVLS
LYSSSIDPFD DDEIALLCNL AGELGLGIGM QRSRQTLAHS EEMLLQAQRL ARLGHFTFDA
ATDVLRGSPT HNELFGIEAG LEIDTDTWLS LIHPEDRQRM ADYSRDHVFR GRQPFDTEYR
VIRRNDGEVR WLHGAGQIEI TANGRVARLF GTSQDITERK HFERRLSRNE KALKEAQAIA
NLGSWTLDIL SDKLTWSDEV YRIFGVAKDQ PLKLGDFLAR IHPDDRDRVQ ADWNAALQGS
PYNSEHRITV DQQVRWVRER AHIRIDDEGR AAFAVGTVQD VTERHEAEEQ LRKLSLAIEQ
TPHSIVITNT AAKIEYVNEA FVRNTGYSRS EAIGSNPSVL HSGMTPGESY NELWQTLGRG
EVWHGEFMNR RKDGSIYEEF AIISPVRQPD GKVTHYLAIK EDITEKKRIQ SELNSYRQHL
EQLVAERTEE LNHAKDEAES ASRAKTAFLA NMSHEIRTPM NAIIGLTHLA QRSTSDPEQN
KRLGKVADAA HHLMSIINDV LDISKIEANK LKLENTDFSL AQLCTAACEL VTQRADAKRL
PVTCIIDPAL PPVLCGDPLR IQQILLNFLS NAIKFTERGK IDIRVQALQK SGDGILIRCA
VSDTGIGIAS DAQRKLFVPF EQGDASTTRR YGGTGLGLAI SRRLAEAMHG EIGVDSKLGQ
GSTFWFTARL SVGAGEQDAG YDQPASTTHQ LGAHILLAED NAINAEVASD LLRGAGLKVD
LAKDGAEALS LARRQHYDLI LMDMQMPVMD GLEATRQIRT LPGWGKIPIL AMTANAFDED
KDTCLAAGMN DHVAKPVAPD VLFAALARWL PTQTSIQIPS TAPQNTSSLL AHIGGLDSNF
GLRAVRGRLD SYLRLLGKFS ENHLDDFSRI RENLASGNLD EARRLAHSLK GVSATLGAED
IQQTAMALEL AIKERHPTEA IEPLIEQSEK AYLSLHQQLA ALKINEQASA NVGDASATAD
LVEHVRRELQ QGEISVQELV RQQAKTLQQV LGSAYPEFEG LVSSFDFEDA LIFLDQYRIK
//
