ID A0A0F2J0K8_9BACT Unreviewed; 907 AA.
AC A0A0F2J0K8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MCHI_002220 {ECO:0000313|EMBL:KJR41883.1};
OS Candidatus Magnetoovum chiemensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetoovum.
OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR41883.1, ECO:0000313|Proteomes:UP000033718};
RN [1] {ECO:0000313|EMBL:KJR41883.1, ECO:0000313|Proteomes:UP000033718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR41883.1,
RC ECO:0000313|Proteomes:UP000033718};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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:KJR41883.1}.
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DR EMBL; JZJI01000575; KJR41883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2J0K8; -.
DR PATRIC; fig|1609970.3.peg.2436; -.
DR Proteomes; UP000033718; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KJR41883.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000033718};
KW Transferase {ECO:0000313|EMBL:KJR41883.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..283
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 342..420
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 415..467
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 548..601
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 646..888
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 592..619
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 907 AA; 102903 MW; 510B5493D2EF9A37 CRC64;
MLDRLLAKIL NISAIVLVVI CLFVSEGASL VIVSFMSYVY HGRITEDYLV TSVIASLFVS
LVVVSMLGFF INRLKSINSQ LIKKNDYIHK ILNSFKHTAI IEADAELNIR FYNTTALLLF
SDMNRDLSGL NLKSLTIGGI NVCRVEDIRE HVDKDIEYTS IVQYQGISGA KHIDVNISKI
YTDECEASEA KDNNGYLLII KDITEQKNIQ KKLLYSEQKF RFMFESSPVM MQTIDSSGSV
SDVNFRWIEK TGYTKKELLG KTANYILQQN FTGKVMDYIR PSSLMEDQCK LFSCRIITKK
QEIIDVLLHI CSAVDPEGMP MSIAAAVDVT QKNAAERALK AQLNFLQVLI DAIPNPVFYK
DVEGRYLGCN KAFEQALGLN KEYVKGKTVY DISPKQLADI YHAKDMELLR TRTLQIYETK
VKYADGSEHD IIFNKAIFSD ADNNIAGLVG IMLDITRRKH IEAQLAQSEL RFRTLIEQSP
LSTAIFTPEG YIITVNKAFT DLWRIDDSSM ENFKQKYCIF KDGELRRRGI MSYVEKGFSG
DFLIIPPIEY EVFIEKTSSA LKRWIRFFIY AVKDANGSVK EAVLIQEDVT AIIHTQAQLD
EKRKELESWN SDLQKKVIEE IEKNRAKEQF LIHQSKVAAM GEMIATIAHQ WRQPLNALGM
IIQDMPEAYH FGELNDDYLE KTVKDAMEQI KFMSDTVDDF RNFFRHDKEK VDFDLIKAIS
SVLTILSAQF TASGIIIKVR CKKDTSAVRF DELKKSQDYQ FCENYITGYP NEFKQVMLNI
LNNAKDAILD RKQSELTNSA DTGIIEIALF TENDNVVNIT VQDNGGGIAP DVIERIFDPY
FTTKQDAKGT GIGLYISKMI IETNMGGRLY AANTAQGAIF TIKLKMSNSK KPSLMAEGSN
SNFGVIS
//
