ID A0A1I5JKV2_9BACT Unreviewed; 519 AA.
AC A0A1I5JKV2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04487852_10654 {ECO:0000313|EMBL:SFO73163.1};
OS Prevotella sp. tf2-5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761889 {ECO:0000313|EMBL:SFO73163.1, ECO:0000313|Proteomes:UP000198673};
RN [1] {ECO:0000313|EMBL:SFO73163.1, ECO:0000313|Proteomes:UP000198673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF2-5 {ECO:0000313|EMBL:SFO73163.1,
RC ECO:0000313|Proteomes:UP000198673};
RA de Groot N.N.;
RL Submitted (OCT-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOWK01000006; SFO73163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5JKV2; -.
DR STRING; 1761889.SAMN04487852_10654; -.
DR Proteomes; UP000198673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR033406; DUF5113.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF17140; DUF5113; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SFO73163.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198673};
KW Transferase {ECO:0000313|EMBL:SFO73163.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..128
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 519 AA; 59618 MW; 9B2E78A814C077DB CRC64;
MKGITLQVEP TETVVKADRV LTLFMLNTLA DNARKFTERG GEVCVSAVET ADYVELSVKD
TGKGIPETEL AQVFNHQVKG GHGFGLMNCK GIIEKYRKIS QIFQVCHLSA ESEEGKGSRF
FFRLPKGIMR LLVVGILLLT SGTLPAYSQR QTANSDIDQA HIFADSAYFS NINGTYARTL
EFADSCRKYL NAHYLSQHPK GSLLMQRQGN ASLVAPEIQW LYDSVSTNYQ IILDIRNESA
VAALALHEWE LYAYNNKVYT QLFKELSADN TLADYCRMMQ QSQSNKRIAI ILLILILMLM
IPAYYMLYYR HRLYNRFRKE RLQQTNLEMA EDELRRAELE DSNLHVSNAV LDNCLSTLKH
ETMYYPSRIR QLADKGETQS MLEVASYYRE LYGLLSEQAL RQTEQVKLHL KKVELYGQEV
LGDEHMLRYL FELLKGDVTV EVKDQQYLLY TIRRADLQIT EEEAANLFSP QMNTIPYLLC
RQIVRDHGEA TNRRGCGIWA KVAEGITWIQ ITLPRYGKL
//