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Database: UniProt
Entry: A0A1W9STN9_9BACT
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ID   A0A1W9STN9_9BACT        Unreviewed;       662 AA.
AC   A0A1W9STN9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B6I20_09725 {ECO:0000313|EMBL:OQX99690.1};
OS   Bacteroidetes bacterium 4572_117.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1971632 {ECO:0000313|EMBL:OQX99690.1, ECO:0000313|Proteomes:UP000192701};
RN   [1] {ECO:0000313|Proteomes:UP000192701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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   -!- 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:OQX99690.1}.
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DR   EMBL; NBLH01000150; OQX99690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9STN9; -.
DR   Proteomes; UP000192701; Unassembled WGS sequence.
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; 1.25.40.10; Tetratricopeptide repeat 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00028; TPR; 4.
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; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50005; TPR; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        362..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          84..117
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          124..157
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          164..197
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          204..237
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          443..662
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          388..419
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   662 AA;  76414 MW;  967A8A1CE9A50C18 CRC64;
     MKIGKSIIVL IFISFISSKI EAQRTAIDSL ENLLQKHAKK DTIRVNLLNK LAYKVHLQDF
     DKTFKYAKEA NDLAEELSFA KGKAESFRFI GIYYYLKGNY FNALEYYQKA LILEEKLDNK
     RGIARCCNNI GMIYMYQDEY LKSLEYLQKA LKLSKKSGDQ IGVSLSSNNI GNTYRAMENY
     PDALEYYQKA LKIKKKLGSK RGVAGTYHNI GKNYKFQGNY PKSLEYLQKS LKICIEIGDR
     SIEARNYTEL GSVYLIQEKV KPAYNYSKKS YLLAKKIGEL NFQKESSEIL AKSCELMGRY
     KEAYRYSVIF KMVNDSIYNE KNTKEIAKLE SRYKYEKEKE LAVIKQQKKD EIYTAEKRRQ
     KIINIFFVTG FTLIIFIAVL VYYNFLQKRK ANHILAGQKS EIEEKNKELF QQNEEIQTQT
     IKLRTTNKKL EAANATKDKF FSIIAHDLKS PFNTIIGFAD ILINDFDDLE NKTKKEYIRY
     IRQGAENTYK LLENLLLWAR TQEGNINFSP EQLNFYLLIN ETRKTLNQFA INKSISIINN
     IPENIHVDAD KNMLSTIMRN LISNAIKFTP KEGTVEIGVE TRHGVSLHEI YVKDSGVGIS
     KEMQSKIFDI GENTSTKGTE NEKGTGLGLI LCKEFIEKHG GKIWVESDIG KGSKFIFTLP
     AI
//
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