ID A0A1Z9QG09_9BACT Unreviewed; 740 AA.
AC A0A1Z9QG09;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CBD91_00905 {ECO:0000313|EMBL:OUX03135.1};
OS Phycisphaeraceae bacterium TMED231.
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae.
OX NCBI_TaxID=1986831 {ECO:0000313|EMBL:OUX03135.1, ECO:0000313|Proteomes:UP000196960};
RN [1] {ECO:0000313|EMBL:OUX03135.1, ECO:0000313|Proteomes:UP000196960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED231 {ECO:0000313|EMBL:OUX03135.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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 -!- 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:OUX03135.1}.
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DR EMBL; NHKC01000009; OUX03135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9QG09; -.
DR Proteomes; UP000196960; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; 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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 122..193
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 200..250
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 327..380
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 393..606
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 627..738
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 676
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 740 AA; 79666 MW; 33BF604B4E0F9BC5 CRC64;
MSMHPKDRLE VSGEAVARLP LVLWETDLEG RLLRPPSGGG VARPEAAADG LVDVLESDVR
LRDAARAAIE GATSAFEQRV GENVYRVSIG PLRDQTGRII GASGVGIDVT AERTAMDTAD
ARDQQIRLLV DTALDAVITC DPESRIVVWN TGAEQLFGWS QAEAVGKRLT ETIIPPEFVE
AHERGMVRFI ETGEGPVLGT RIEIEAQDRN GRRFPVELSI NPIPTSSGLS FSGFIRDISA
RKASERATRE GEERLSLALD AIDAGAWDYT LASNGRLEAS TVSSRTTAIL GPDANRKPPD
RASLHPEDRQ EVADRWASIC SGRAEEFTVE YRLHTEDGRT LWMSEHGRAF ESDEEGAARR
VVGVISDISR RRAMEETLLA TQKTDALGAI AGGFAHDLNN VLAAIRGHAS LASLEAGIPP
EVSESLEVIQ AAVTRGRSLT QNMMMLGSPT RIRRTVVDAS KICRETLALV RPAVPASISI
SERFEAGEHR ILADGNQFQQ AVLNLVVNAR DAVSGSGSIE VAIDRMPATT DAPPRLAIAV
RDDGGGMDDE VRRRAIEPFY TTKGRAGNGL GLAMVKNFVE GCKGTLEIES TPGRGTVVSL
VLPEVEAAVD QGGFNAASSG AARSASRVLL AEDHPLLRPM LLEAMTVGGF EVRHAADASK
ALEIADSWSP TVLVLDVNLP GDTGDVIAAR IRERRGEDVP VVFITGNNDF EAPEWKAMKL
LRKPFGLDEL MTAIDQLITD
//
