ID A6SUF8_JANMA Unreviewed; 788 AA.
AC A6SUF8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=mma_0215 {ECO:0000313|EMBL:ABR89942.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR89942.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR89942.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR89942.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89942.1; -; Genomic_DNA.
DR RefSeq; WP_011979441.1; NC_009659.1.
DR AlphaFoldDB; A6SUF8; -.
DR STRING; 375286.mma_0215; -.
DR KEGG; mms:mma_0215; -.
DR eggNOG; COG4252; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_016084_0_0_4; -.
DR OrthoDB; 9121563at2; -.
DR Proteomes; UP000006388; Chromosome.
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 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; IPR007890; CHASE2.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017181; Sig_transdc_His_kin_CHASE2.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PIRSF; PIRSF037347; STHK_CHASE2_PAS_prd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABR89942.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006388};
KW Transferase {ECO:0000313|EMBL:ABR89942.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 568..786
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 788 AA; 87132 MW; 0DCE04DD7A049BBB CRC64;
MKIRWLSPLV RHLALREWLM LFIGLLTLAI ALGWQNGLGR LDQSLYDLFL SVDSKPVRED
IIIVAIDDYS LAELGRWPWS RKLHADLINK LNKAKPRAIG LDVILSEEST PQADGQLAAA
IMQSQHVVLP VVLSNAGQGL RAGLPIPLLA NSAHTLGHIN LEHDSDGVVR SVFLREGQSG
KNWLHFSAAL LSTGSGMQYN GTKALPAPTS ASLIDTWQRG DQLYIPYEGG IGHFKSVPYV
SVLRGEVPDE FFTDKYVLVG ATALGMADSY PTPVSGNSGA MPGIEINAHV LASLIDGEEI
HIAAAWQTAF FNAIPVFMAL LGYLLLSPRF SLFATGIWIL VTLVTSYIGL RMGIWIAPAA
AVITLIISYP LWSWRRLEAA ITYLGQEFTR LDQEPHLLPE EKTAVSQNEM ADVLEQRITA
MKNAARRVRD LRQFVSDNLD NLPDATLVTS VEGQVLLANK HANDYYRSLG IDDVLGRNII
DLLAQLKNPQ PVDQAANLSF DWPDLLDIQA SQSLHNGIST QDQKGRDLLV KSSPCNSATN
LLTGWIVSVL DISTIRAAER SRDETLRFLS HDMRAPQASI LALLELQSET SSALPQAELF
SRIEKASRKT LGLADNFVQL ARAESHEYRL EEVDFQDLLF DATDEMWSLA KSRHITVQME
ISDGEYPVKV DRTLMTRALA NLLSNAINYS PDHTSIECSV RLEQEGPEQR VVCRILDHGY
GIADADQGKL FLRFQRVDLP NQPRHDGVGL GLVFVKTVIE RHQGDISFIS QAGVGTSFTL
MLPVCHEV
//
