ID A0A0P1H3T9_9RHOB Unreviewed; 461 AA.
AC A0A0P1H3T9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kinB {ECO:0000313|EMBL:CUH89660.1};
GN ORFNames=PH5382_03608 {ECO:0000313|EMBL:CUH89660.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH89660.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH89660.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH89660.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-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};
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DR EMBL; CYSG01000024; CUH89660.1; -; Genomic_DNA.
DR RefSeq; WP_058335738.1; NZ_CYSG01000024.1.
DR AlphaFoldDB; A0A0P1H3T9; -.
DR STRING; 1712645.PH5382_03608; -.
DR OrthoDB; 9784218at2; -.
DR Proteomes; UP000050782; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Transferase {ECO:0000313|EMBL:CUH89660.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..458
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 215..242
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 461 AA; 49993 MW; 9785B32FB044DB27 CRC64;
MLNSLSGRFL VLTTVFVMLA EVLIFVPSIS RFRLDYLSER LERAQIASLA LLADDMLETE
LEAELLENAG VYNVVLRRDE IRQLMLSSPI PQAIAGTYDL RMANAFTLIG DAFQQLASPE
NRIIRVIGAP VRDAGLLIEI TIETAPLRMA MIDYGVRILL LSAVISIFTA LLLFAAVRVF
LVRPIKGVVG YMQRYAAAPE DARGIIQPNA GVSELREAEE ALLQLQTELT HALRQRERLA
QLGGAVAKIS HDLRNILTSA QLFTDRIEMS EDPLVRRLAP KLVNSITRAV SLCEGTLAFG
RAEEPAPTFA HVPLCELVND IVESESLAAT DTEVSIVNAV PKGLMLRGDA EQLFRVVMNL
VRNARQAIVS TGQSGQVTIS ARDEDDAWWI TVQDTGPGLP KKAQDNLFTP FQGGTRKGGS
GLGLAIAAEL IRGHGGVVAL GETGPAGTIF EIRLPKGDGA I
//
