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Database: UniProt
Entry: A0A0F3GWQ4_9BACT
LinkDB: A0A0F3GWQ4_9BACT
Original site: A0A0F3GWQ4_9BACT 
ID   A0A0F3GWQ4_9BACT        Unreviewed;       589 AA.
AC   A0A0F3GWQ4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MBAV_001467 {ECO:0000313|EMBL:KJU86336.1};
OS   Candidatus Magnetobacterium bavaricum.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Magnetobacterium.
OX   NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU86336.1, ECO:0000313|Proteomes:UP000033423};
RN   [1] {ECO:0000313|EMBL:KJU86336.1, ECO:0000313|Proteomes:UP000033423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM-1 {ECO:0000313|EMBL:KJU86336.1};
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:KJU86336.1}.
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DR   EMBL; LACI01000642; KJU86336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F3GWQ4; -.
DR   PATRIC; fig|29290.4.peg.1946; -.
DR   Proteomes; UP000033423; 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; cd00075; HATPase; 1.
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; 1.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF82; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE ARLS; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KJU86336.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033423};
KW   Transferase {ECO:0000313|EMBL:KJU86336.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          241..291
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          362..583
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   589 AA;  66801 MW;  F2144A892253BCF0 CRC64;
     MNGYKVKRRY WLIVVLAIVV LVVTSISGML LYQTAVKVQS QRLSAAAEFS ARLVEVNIEQ
     RLRKTERRDW QTLSIIEKEV IEEINQIHQK SQQNSGQIGE FVWGRWEGKE IVFLLPVHHS
     QKKSIPLDSD LAEPMRLAIK GQRGVVIGLD YRGEKVLAAY EPLRIIGRDY GFVTKLDMSV
     VRVPFIRVGL VTFFLAIAAI LLGAFAFLRI TDPMLRRMQE SESRFRCLVE QSLVGICIIQ
     NGKFTYVNPR FAEIFGYDKT EELLGRTPAE LACADDREMV SENIRKRISG EVSFAHYCFC
     GVKKDGKTVQ IEVHGSRMEI QNVPAIIGVL LDITRRTEDG RRLQQLKVAE EASRTKNEFL
     SLVTHELRTP LNGITGFAQT LMDAHSDGWL MQQKGMLGDI LEKILQSAFH MASLIEGLLE
     FSRIEAGQLS IQYEAIDLRQ PLDIVKSNLS EKLREKELEF KVQIPVDLPL IHAGLKQLTQ
     VLFNLIGNAI KFIDRKGIVT VRAMEEGAMV LVIVQDSGPG MDEETLRHVF EMFWRGNKAK
     SVEGVGLGLA ITKKIVETMD GEIWVKSELG VGSTFYFTLK QWRKNAENY
//
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