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Database: UniProt
Entry: A0A1U7EYQ3_NATPD
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ID   A0A1U7EYQ3_NATPD        Unreviewed;      1008 AA.
AC   A0A1U7EYQ3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=NP_4606A {ECO:0000313|EMBL:CAI50394.1};
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780 {ECO:0000313|EMBL:CAI50394.1, ECO:0000313|Proteomes:UP000002698};
RN   [1] {ECO:0000313|EMBL:CAI50394.1, ECO:0000313|Proteomes:UP000002698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC   NCIMB 2260 / Gabara {ECO:0000313|Proteomes:UP000002698};
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50394.1; -; Genomic_DNA.
DR   RefSeq; WP_011324009.1; NC_007426.1.
DR   AlphaFoldDB; A0A1U7EYQ3; -.
DR   STRING; 348780.NP_4606A; -.
DR   EnsemblBacteria; CAI50394; CAI50394; NP_4606A.
DR   GeneID; 3702113; -.
DR   KEGG; nph:NP_4606A; -.
DR   eggNOG; arCOG02333; Archaea.
DR   eggNOG; arCOG02340; Archaea.
DR   eggNOG; arCOG06408; Archaea.
DR   HOGENOM; CLU_000445_114_71_2; -.
DR   OMA; MIAERDW; -.
DR   OrthoDB; 3369at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 6.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 3.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAI50394.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAI50394.1}.
FT   DOMAIN          159..231
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          234..286
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          283..354
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          354..408
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          485..538
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          555..609
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          611..663
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          664..723
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          801..1008
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          62..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          392..419
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        66..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1008 AA;  113461 MW;  6A2C3CC61FBA7C09 CRC64;
     MSEESITDPD SSQGAAAANS THEAFLCATS DAAFLVDAER TDDGYEFTLL EHNDAYRRLT
     EHTSSHDTAR NVIPEPATTQ QQSAHHYCRR CVEEQTTLQY AASFATPSAT DRWETTLTPV
     VEDGAVDHIV GVVESPTESP REQTQPKDSH ERRHSPEHIH QRLESALDAA DAGVWEVDPE
     TRTVYCDDRA CSIFGLSPTS FTGTWTEITE CVHPGDWDDF ETAYDQAVGD PSGREVEFRV
     QSNGESANWV RVHAQPVAST DGTPDRLVGT IRDITDEKRR SRKLEQFREA AEQTGHAVCL
     LDADGTIEYV NPAFEAITGY DAATAIGEPI QLLRSDAHDR SFYVELWQTI LAGERWEGEA
     IKERADGEEI TFSQTVSPLT DDKGDPNGFV LVARDITEKK QREQEINQLR ERLELAIKGA
     NISVWDWDIE SNTIELHNSS AIVSRQDSDN SRIKQKEWER RIHPDDIDGI WETFEDHVVE
     ESEYYEAEYR VLAGDGDWRW VRDLGQVIER DEDGEPIRAV GVQLDIDDKK RAWITVEQER
     DMFTEGPVVL FRWRDEPGWP IEYASDNVEA LLGYEPKELT DDIGSFAEII HDDDIGQARQ
     KAEQARKRGR GSHEYRVVTA DGETRWVFEH TKFVQHNTED RRIALGYVVD ITERKRREQE
     LETARNELRR IIDLVPDPIH VRDKDGRFIL ANEATAELYG TTPEALNGKD DDDLPFEVQH
     SSDCTEDVAA VIDSGERIEA EEELTTAHGD DKTLELTRIP YETTRADTPT ALTYARDVTA
     LKAYERTLEQ QRDNLETLNQ VVRHDIRNSL QLVLAYGEML EAHVDGDAAD FVEHVTEAAS
     DAVTITETAR DVTEVLLRSA DELTAVNLTC VLDDQVTSIR ASHERATIDI EGSIPDCAVR
     ADEMLESAVR NLLSNAIQHN DNDHPRVTVA ATADDETVEL RIADNGPGIP DDQKDRIFQE
     GEKGLDSDGT GLGLYLVDTL IDRYDGEIRV EDNDPRGAVF VVELQQAD
//
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