ID A0A1L8CK54_9PROT Unreviewed; 668 AA.
AC A0A1L8CK54;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MMIC_P0168 {ECO:0000313|EMBL:GAV19239.1};
OS Mariprofundus micogutta.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=1921010 {ECO:0000313|EMBL:GAV19239.1, ECO:0000313|Proteomes:UP000231632};
RN [1] {ECO:0000313|EMBL:GAV19239.1, ECO:0000313|Proteomes:UP000231632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ET2 {ECO:0000313|EMBL:GAV19239.1,
RC ECO:0000313|Proteomes:UP000231632};
RX PubMed=27766355; DOI=10.1007/s00203-016-1307-4;
RA Makita H., Tanaka E., Mitsunobu S., Miyazaki M., Nunoura T., Uematsu K.,
RA Takaki Y., Nishi S., Shimamura S., Takai K.;
RT "Mariprofundus micogutta sp. nov., a novel iron-oxidizing
RT zetaproteobacterium isolated from a deep-sea hydrothermal field at the
RT Bayonnaise knoll of the Izu-Ogasawara arc, and a description of
RT Mariprofundales ord. nov. and Zetaproteobacteria classis nov.";
RL Arch. Microbiol. 199:335-346(2017).
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:GAV19239.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDFD01000001; GAV19239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8CK54; -.
DR STRING; 1921010.MMIC_P0168; -.
DR Proteomes; UP000231632; 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 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; 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; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 40..110
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 114..166
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 163..208
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 234..288
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 301..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 547..663
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 150..177
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 598
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 668 AA; 74421 MW; AD17D6718670CAF1 CRC64;
MVSLYMIIMI SVARKSHDSN IQNIRLRIDS NLHEKELLHS EKRFRDISMS MADWVWEVDA
SGHYTFVSGK VKELLGYEPD EVLGKTPFDL MNEQEAVRVA AMFQEIVDKR APVIDLENWC
KGKAGKEVCM LTNAVPVLGE DEELLGYRGV DQDITERKHV ENELRKLSRA IEFAGESIVI
TDQHGVIEYV NPAFSRMTGY SVDEAIGEMP SMLKSGEQDE AFYQLFWSTI TSGKVWQGSM
VDRRKDNSTY NSMMTVAPIM DDSGEITHFV AMQMDISEYE ALEARFQQSQ KMESIGTLVG
GIAHDFNNML AALLGNLHLA RRVAGDDPKM MDRLNRIETV SQRAADMIAQ LLTFARKGKV
EMAPLPLAPF MKELFKLARP SIPESIDMKL ELGGDDIIVV GDVTQLQQVL LNLITNASHA
LEAVSEPEII VGFKTYRPGI RFRQVHADVD AKHLAVMYVK DNGCGIADHI LDKVFEPFFT
TKEQGKGSGL GLAMVHGAIK THKGAVEIDS KLGCGTTISL FLPLEQDLNI TGIQSEVSAL
ERGAGEGILL VDDEELVREV NSEVLEDLGY HVFTAEDGMH AQQVYEQHAS DINLALVDLV
MPKVGGMELL AWLRHQDKTL PVILMTGYDR EQVLPATATP KQCVVLNKPV DISKLSQAVR
NMLEKQAD
//
