ID W6KD38_MAGSQ Unreviewed; 573 AA.
AC W6KD38;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MGMAQ_3328 {ECO:0000313|EMBL:CCQ75159.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ75159.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ75159.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ75159.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
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; FO538765; CCQ75159.1; -; Genomic_DNA.
DR RefSeq; WP_052716466.1; NZ_FO538765.1.
DR AlphaFoldDB; W6KD38; -.
DR STRING; 1288970.MGMAQ_3328; -.
DR KEGG; magq:MGMAQ_3328; -.
DR HOGENOM; CLU_475526_0_0_5; -.
DR OrthoDB; 7313492at2; -.
DR Proteomes; UP000032733; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16921; HATPase_FilI-like; 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; 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; 1.
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; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CCQ75159.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000032733};
KW Transferase {ECO:0000313|EMBL:CCQ75159.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..282
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 285..337
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 355..569
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 573 AA; 64857 MW; B3071D89FC56E05D CRC64;
MKLSPAWAAL IGILTVLTLL VGVVYIGAIH QVRTILEDDI QDSLRSDLLT LEQAAREMLL
KHHYENVESM FLDWAERTAP VSEFVGRAPN GFAIATFNRP TGSLETRRME HRILHEETLL
LTLSVTYDLS SVDKRVKSLR ILILAVFPVS VLFLGGILWE TVRRSALVPM ERAQKDLRRY
QDHLESMVEE RTHELEDEVR IRSQAEEALR NHSAFLDTLL EAVPAPVFFK NDSMVYIGCN
RAFENFIGMD RNDILQRTVF EIAPPDLAEI YHQADQALFD MGGTQVYEAS VKHQDGRYRD
VIFHKAVFQK ANGEPGGIIG LMVDISDRKN VERDLAQRTR KLEWSNAELK QFAYVTSHDL
QEPLRTVSSY LQLLQNRYGD DLAPEAHEFM DFAIGGASRM SRLINDLLAY SRITTHPQDQ
EQADLNHLLE NALANLTVAI DESDAKVTHD DLPTTMGDPG QLSRLLQNLI GNAIKYRDPD
RSPAIHIEAK RGDGEWILSV SDNGIGIDSA HFHKIFQIFQ RLHQDEEYGG TGIGLAICKR
IVERHGGRIW VDSEPGCGST FCFSLPDENQ TFD
//
