ID A0A109RUK3_9BURK Unreviewed; 756 AA.
AC A0A109RUK3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VN23_03605 {ECO:0000313|EMBL:AMC33747.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC33747.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC33747.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC33747.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-2016) 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; CP014222; AMC33747.1; -; Genomic_DNA.
DR RefSeq; WP_046353176.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A109RUK3; -.
DR STRING; 1236179.VN23_03605; -.
DR KEGG; jab:VN23_03605; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000069577; 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 CDD; cd00130; PAS; 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; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..364
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 368..420
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 544..755
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 756 AA; 84581 MW; 58780B03728A01D1 CRC64;
MITSSLMRRI GQHWLWWLAY IAISLVLLAL TSFVWLDYRQ ARNAQDTVLS QDLLWQEQGL
RLHLQTNQNA IENLAYGIAA NALREEDFRA RSDSLLRASP EMLSVDYVNS SGNRVWGLPA
YSSRPQSLVP LDDPFLLEVL DGAATLGYVL YSNVIMAGEP KVAQVVLVVP IFKGTVYLGS
VLAAYALPAI LQQRVPWWMV QRYDLSLLDG KGNVLAPHDA MQNPSGISRS VGFEPLGHGL
KLRASVRHEK TSVTQLWLLG VVFVLLVALL WALSLLRKRM QQRQHAEGAL RDEMRFRAAM
EDSLTTGLLA INTSGHLIYA NLAFCSMVGR TQAELLGKSS PMPYWAPEEL SVCAAAWNSL
LSGECPVSGF ALRFMRRDGE RFDVRLYSSR LVDGRGEHRG WMASLYDVTE LKSEREALAE
SRKQLLTVLE GLDAAVSVFD VDNGVVRYRN RHHSYTFPML ADGECCMWPL LPLGEATVER
QDPISGRWFL VQRRRIQWVD GHVVWLEIAA DITERRQKAE EDRSREAKLQ HTARLVSMGE
LASSLAHELN QPLAAIAGYA AAGEEILSRD EKSSVRHILS KMGEQARRAG QIISGIRNFS
SRRASRSEPC DFAELLAVPM QLLEPMARKY QSRIVLDLVQ PLPKVMGDGV MLEQVLFNLI
KNGMEAMIDT PVEQREIKVT AYESKDCLEV CVADRGSGIE NPALLFQSFY TSKPEGMGIG
LNICRSVIEQ HQGHLKIQAN PEGGSCFVFR LPIVLS
//
