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Database: UniProt
Entry: F4G8R4_ALIDK
LinkDB: F4G8R4_ALIDK
Original site: F4G8R4_ALIDK 
ID   F4G8R4_ALIDK            Unreviewed;       606 AA.
AC   F4G8R4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Alide2_0930 {ECO:0000313|EMBL:AEB83341.1};
OS   Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Alicycliphilus.
OX   NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB83341.1, ECO:0000313|Proteomes:UP000007938};
RN   [1] {ECO:0000313|EMBL:AEB83341.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RX   PubMed=21742888; DOI=10.1128/JB.00365-11;
RA   Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA   van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA   Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA   Smidt H., Stams A.J.;
RT   "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL   J. Bacteriol. 193:5028-5029(2011).
RN   [2] {ECO:0000313|EMBL:AEB83341.1, ECO:0000313|Proteomes:UP000007938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14773 / CIP 107495 / K601
RC   {ECO:0000313|Proteomes:UP000007938};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA   Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT   "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL   Submitted (APR-2011) 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; CP002657; AEB83341.1; -; Genomic_DNA.
DR   RefSeq; WP_013721501.1; NC_015422.1.
DR   AlphaFoldDB; F4G8R4; -.
DR   STRING; 596154.Alide2_0930; -.
DR   KEGG; adk:Alide2_0930; -.
DR   eggNOG; COG3221; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_011260_2_0_4; -.
DR   OrthoDB; 8559580at2; -.
DR   Proteomes; UP000007938; 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; 3.40.190.10; Periplasmic binding protein-like II; 2.
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   Pfam; PF12974; Phosphonate-bd; 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   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AEB83341.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007938};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:AEB83341.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..606
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003308156"
FT   TRANSMEM        311..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          379..596
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   606 AA;  63952 MW;  15BAAFDA7D494845 CRC64;
     MKRGVFASRR VLGVLLLCAA AARAEVRLGA LAVLEGEDTR RQWQPLADGL QRALGVPVRL
     QALAPAALEQ AVARGALDFV VTNPGHYVAL EARHGATRIA TRSAGAQGDP AHAVGSAVVV
     RADAPGPPAT LAALRGWRVA AVAEEAFGGY QLAAVEWLRQ GVDAEAGGLR RVFTGYPMQR
     VAQAVLSGEA DAGVLRTCLL ELWERDGVVP AGALRVVPAD DDGGTGAPPG CRASTPLYPG
     WAFAALAGTP PELSRQVLLA LLAQPGESGA LDGVWTVPAD YQRVHDALRL LQVEPYAFLR
     ETRLQALLHR YWGVAAALLA LALVGVAYLL RVEVLVKRRT AELTHSLHER ERLARQNAQH
     QEALGHLSRL SILGELSAML AHELNHPLAT IANYAAGLRR RAARGDLAPQ DLERALRDIA
     HESERAARVI GGVRALARKR VPDRVAIDPR ALVGEALTLL GGWQPQAVRV ACAPGAEALR
     VRGDAPQLLQ VLLNLLQNAR DVHRAAGCEG EPIGVEIAPE DGCLALAVRD HGPPLSPEAL
     ALLFTPFHTT KPDGLGLGLS ISRGIAEAHG GALHARPVPP HEGGGMRMVL LLPLAQPEAA
     DGDTPA
//
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