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Database: UniProt
Entry: B4RIF5_PHEZH
LinkDB: B4RIF5_PHEZH
Original site: B4RIF5_PHEZH 
ID   B4RIF5_PHEZH            Unreviewed;       447 AA.
AC   B4RIF5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=fixL {ECO:0000313|EMBL:ACG80130.1};
GN   OrderedLocusNames=PHZ_p0187 {ECO:0000313|EMBL:ACG80130.1};
OS   Phenylobacterium zucineum (strain HLK1).
OG   Plasmid pHLK1 {ECO:0000313|Proteomes:UP000001868}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG80130.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG80130.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|Proteomes:UP000001868};
RC   PLASMID=Plasmid pHLK1 {ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; CP000748; ACG80130.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4RIF5; -.
DR   KEGG; pzu:PHZ_p0187; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_39_5; -.
DR   OMA; NGIIMRI; -.
DR   Proteomes; UP000001868; Plasmid pHLK1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.250.2580; -; 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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF47; COMPONENT HISTIDINE KINASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:ACG80130.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:ACG80130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW   Transferase {ECO:0000313|EMBL:ACG80130.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          77..147
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          145..204
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          224..439
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   447 AA;  48057 MW;  E4915BB339971EA6 CRC64;
     MGIAGVYGGG VPGVVATVVG IGYGLLWGSA PTLEPAAMLF GRTVAFAVIG LGAAWVGERR
     RIAIRSAEKV NADLVAQQAH LRSILETVPD AMVVIDSRGR IQSFSTAAER LFGYSAGEVV
     GNNVNMLMPA PYRENHDTYL ERYLRTGERR IIGVGRVVVG QRKDGSTFPM ELSVGEMQSG
     ASRFFTGFVR DLSERQLTEQ RLHELQSELV HVSRLTALGE MSSALAHELN QPLSAIANYL
     TGAQRLLARQ KDATSQKVNG ALDKAVAQAL RSGDIIRRLR EFVARGETSQ RPESVAKLVE
     EASALALVGA RQLGVRVVFD LDERVDYVLV DKVQIQQVVL NLIRNAVEAM TDSPRRELTV
     ASAPGPDGMV DISIADTGPG IDKDVAGKLF QPFVTTKAQG MGVGLSICRT IVEAHGGRIW
     AEPNRGGGTI FHLTVAEATA EELAHAR
//
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