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Database: UniProt
Entry: H0EAF8_9ACTN
LinkDB: H0EAF8_9ACTN
Original site: H0EAF8_9ACTN 
ID   H0EAF8_9ACTN            Unreviewed;       487 AA.
AC   H0EAF8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   03-MAY-2023, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PAI11_38320 {ECO:0000313|EMBL:EHN09285.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN09285.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN09285.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN09285.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
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:EHN09285.1}.
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DR   EMBL; AGUD01000295; EHN09285.1; -; Genomic_DNA.
DR   RefSeq; WP_007578287.1; NZ_AGUD01000295.1.
DR   AlphaFoldDB; H0EAF8; -.
DR   PATRIC; fig|1097667.3.peg.3797; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF48; TWO-COMPONENT SENSOR HISTIDINE KINASE-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EHN09285.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW   Transferase {ECO:0000313|EMBL:EHN09285.1}.
FT   DOMAIN          22..141
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          299..472
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   487 AA;  52352 MW;  733F81EFF9701FA6 CRC64;
     MGDDFSDDGV PATVEQLRAV DLFDGLDDAQ LAAWASVARV QEVPAGTVLA EQGRQPAGVH
     LLLRGSVQNW LVEGERSEPI GRQQAPTWMG AVAVIIDGAH AVRMQVEEPS LVALLPADEF
     RRITYEQPLV RERVMSKVSP VVHRIAAVEQ NRERLAALGT MAAGLAHELN NPAAAARRAA
     ADMAEAIETV NGALISLVAA GVERAEAAQL IELQQQAVQR SASCSALDAL DAADAEDELR
     DALEDAGVGE AWRIVEPLAR ARVDAAWLER VRGLAGEATD AVVRWVAATL SAQGLARELQ
     ESTARMSELV GAVKSYAYVD RGEVVQVDVH EGLETTLTVL GHKLKQTAIE VVRDYDRTLP
     PLMVRGPELN QVWTNLLDNA IQALGERGTI TLATRRDGPC ALIEISDDGP GMPPEVRDRV
     FESFFTTKDV GQGTGLGLTT ARSIVVDRHH GSMTVDSEPG RTTFHVWIPF ESAADDETLI
     PVEPNAA
//
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