ID K2G3P4_9BACT Unreviewed; 1098 AA.
AC K2G3P4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ACD_10C00256G0002 {ECO:0000313|EMBL:EKE17825.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE17825.1};
RN [1] {ECO:0000313|EMBL:EKE17825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:EKE17825.1}.
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DR EMBL; AMFJ01003573; EKE17825.1; -; Genomic_DNA.
DR AlphaFoldDB; K2G3P4; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 3.30.450.20; PAS domain; 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; IPR007895; MASE1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..338
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 368..420
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 547..600
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 714..936
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 964..1080
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1013
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1098 AA; 122077 MW; D0DA467306B63A92 CRC64;
MSKNSASSSW PRQFGIAAVY LFLGLIIHRD VAANGLVNIV WPGSGVALAA VLIGGRRYLW
SIAAGALLLY LLLTDSLAVA LGLMLANVLG AWFTAWLVAK AGPPAMLLRD LRGYLHLLLR
GAAGSLLTAA IACAALLPVS NANYLSNLQH WWMGDVFGVA LVTPLILAWW QDRKISFTTR
QWLEIVLLAG TTIFIGQVVF LDWLTNYLSN TPKGYVMFFF AAWCAIRLGA RSVSLIVLII
ATQAMASADL EVGRFSDEIA KAELNNYWAY MMTLAGLVMA IVISIRTSHD AMKLALQRDK
ALNAAANGVM ITDRNGRIEW VNQSLCQLTG YTEAEMLGLN SRELFKSGKH ETPYYESLWG
TIMGKKVWHG EILNRRKDGS LYHEEMTITP LLDAHGEIEN FVAIKQDVSQ RIAEQQALVY
SEALFHSLFQ NMSSGVAVYA AVDNGNDFIF KDINPAVERL ENIQRDTVIG QRLTQVFPGI
KEFGLLEVLQ RVWQSGQHEY FPLSFYRNER ITGWRDNHIH RLASGEVVAV YDDITARKQS
EMALMISNQR ITSLLDSMAE GAYGVDLKGN CTFVNQSFLR ILGYERPEQI IGQHIHELIH
HSHADGRHYP AQDCRMYHAY RRHENIHCDS EVFWCRDGTA KAVEYWSHPI FTDGKVAGAI
ATFIDITERK RNAAELAQHR NHLENLVEMR THDLSIAKEA AEAANRAKSA FLAVMSHELR
TPMNAIMGMT DLALRRATDP RQINQLDKAA KAADHLLALI NNILDLSRIE AERLTLEEIP
FQLGVVLENL NSMIGQTASD KGLQLILDIA PELSSRALTG DPLRLGQILL NLAANAIKFT
EQGSVTVRTL LTEESPSHLS LRFEVIDTGI GISPEDQKRI FNSFEQSDGS MTRKHGGSGL
GLAISKRLVE MMNGRIGIES KHGNGSTFWF TARLKPAENF FAAPSKPHNR TAEEELRSTY
AGTRVLLVED EPINQEVSQA LLEAVGLQVD LADDGIAAVN LAKRTNYALI LMDMQMPRMN
GIEATEAIRA LPGRQHTPIL ALTANAFNED RERCHKAGMN DHISKPVDPE KLFETLLNWL
SLDSSVDRSS LSGKPCEH
//
