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}.
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; 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
//