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Database: UniProt
Entry: A0A1I5JKV2_9BACT
LinkDB: A0A1I5JKV2_9BACT
Original site: A0A1I5JKV2_9BACT 
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};
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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
//
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