ID D8PAQ8_9BACT Unreviewed; 910 AA.
AC D8PAQ8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIDE0542 {ECO:0000313|EMBL:CBK40317.1};
OS Nitrospira defluvii.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK40317.1, ECO:0000313|Proteomes:UP000001660};
RN [1] {ECO:0000313|EMBL:CBK40317.1, ECO:0000313|Proteomes:UP000001660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT "A Nitrospira metagenome illuminates the physiology and evolution of
RT globally important nitrite-oxidizing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(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; FP929003; CBK40317.1; -; Genomic_DNA.
DR AlphaFoldDB; D8PAQ8; -.
DR STRING; 330214.NIDE0542; -.
DR KEGG; nde:NIDE0542; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_323834_0_0_0; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000001660; Chromosome.
DR GO; GO:0005524; F:ATP binding; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 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; 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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001660};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 137..207
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 272..310
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 343..395
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 701..909
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 910 AA; 99352 MW; 62548851CA4FCBE1 CRC64;
MRPPVLIVDD DPDIRESLTD MLGHEGYLVH SAASGTEALQ QAKQTRYDAA LLDIQLPDLN
GLSVLKVLME LDASLPVIIL TGNVTPENTI GSLAKGAFAY LTKPYNSQEL KAILRRAVSV
KGLTVRAEHV EEALQASEER FRALVESATD AMVLADQSGL IIWWNGAAER MFGYTKEDAL
GRPLTIMMPE RFRAAHAAGV TRLAQGGTAT IIGHTIELVG LTKTGDEFPI ELSLASWRAS
DGMFFSGIIR NIARRKRAEE SVVRLSHQNA LILDSAGEGI FGLDPQGCVT FANATAARIL
GWSAAELIGK PLAPLLYRIA NGNAARSPDP FCLCAALHDG AVHRIQNEAF ARKDGSLFPV
QYVTSPIRER DRLVGAVVVF QDISARKQQE NLQQAQLSVS HILAQAGTVE EAIPQLLHVA
GTMGAWDMAL LWQCGRMGDQ LTCHGSWIRP SHRWDEFLSV CRNSEFPPGM DFPGIAWASK
LPLWIPDALT DSRFTRAPTA SRLGIHGACI VPIRTGSIIH GVLELYTEQR RPSDSHLIQI
LADTGMKIGQ FIDRTRAAQA LRAAHRTTQS LLASLPGAIF LCGSDLQVQY ANALAHQYFA
LPGESLIGRP LCECLSLSEP ALQRQVVEWN THTADSPHRL SECECEVAAR LYRYRFFPVS
TPESPQYQVG ILLWDITDDK RLQDELIQAE KLSSLGTMVS GMAHEINNPA QAILSMAELI
QEEDDPDTVK QFAADIVGYA RHVSTVVRDF AGYARAAGRD GETEIDVAER LLEAVKMVRR
GPHFGQVEIA TQFDAPVFLR ARKGEIDQVF VNLISNATQA MEGIGCLTLT TGQDGRWIQV
TIADTGPGIP ASIRPRIFDP FFTTKTAGKG TGLGLSIVHK IVIKYAGTIT VESTEGGGTT
FRLRFPALVQ
//
