ID A0A2W7NDY8_9BACT Unreviewed; 1122 AA.
AC A0A2W7NDY8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LX69_02293 {ECO:0000313|EMBL:PZX14964.1};
OS Breznakibacter xylanolyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Breznakibacter.
OX NCBI_TaxID=990 {ECO:0000313|EMBL:PZX14964.1, ECO:0000313|Proteomes:UP000249239};
RN [1] {ECO:0000313|EMBL:PZX14964.1, ECO:0000313|Proteomes:UP000249239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6779 {ECO:0000313|EMBL:PZX14964.1,
RC ECO:0000313|Proteomes:UP000249239};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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:PZX14964.1}.
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DR EMBL; QKZK01000018; PZX14964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NDY8; -.
DR OrthoDB; 9797097at2; -.
DR Proteomes; UP000249239; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07494; Reg_prop; 7.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 4.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PZX14964.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249239};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PZX14964.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1122
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016051831"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 906..1122
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 833..867
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1122 AA; 127856 MW; 619CAABF21058568 CRC64;
MLRCLIILLS FTMIPLTWSQ SSGFQFNSLD KEDGLAGNNT RCFLKDSKGF IWIGTAEGLS
RYDGYTFKNY THNLSDSSSL RDNNINAIAE APDGRFWITA GDYFEIFDPR TDRFDHSQTL
FDEQLQIPLV SRTAFATDDA GNIWIGNTSI GLFRYHQQLK IVEKISTATP GHVHPTDTIT
AIKADTDGNI WVCDYRGQVL CFSPNGVIVK QVQIPQLPNN FPQLFIDHQN TIWIYDMNSN
YGLLRYLPST GGLSMVSHES TKGRLQSNIV TSVIDVNDEN IWVGTDHGGI QVINKNTLNI
SHIKSHPHRK RSLCSNSITN IYLDREGFIW IGSFKKGFSY YHPGLFNFNL YQINLDHSSC
DALNDVDNFA EDASGNLWIG TNGSGLVYYN RKNDTFTQYK HDPNNVNSLS NDTVIGMHMD
RRGRLWAGTY MGGLVCYDQG RFTRFLNNPD KPLSLSDNRV WDICEDRDGM LWVSTLQGGI
TIIDPHKNAV VKVIKGLDSP LRSYVVFDIN KGRLGELWIA TVDGLRMYNP DKDAWQYYDQ
QSSIKLSHNT VRTSIEDHSG LIWIATADGL NLLDRATGNI TVLRTDDGLP SNNILTLLED
NQGRIWMSTT HGISMAERKN INNIDHVHFT NFDDKDGLQG KVFNEKSAFK TRQGEMIFGG
SQGFNIFDPD KVALQNLHAN TEITDFQVFN QSITPAIAID GHIFSDQTIA YTSVVELEHQ
FNLFSIEFAS LNFFFPERRK YQYLLEGFQN DWLTTESSNR RITYTNLNPG LYTFKVKSTN
TDGSWNDTYS SLQIKILPPW WDTLLFKILA VSAVLALMIV AYYARFYSIQ HQKRKLEQQV
TERTRQLNDL NRELTIQQAE ISLQNRELTD HRTHLEEMVE KRTAELEKAL LKAESADRLK
SAFLANMSHE IRTPMNAIFG FSALLRDSEI TPEENNRFID IIQSSCDTLL VIINDILDIS
KIEANQLEIN KRKSNIHDIF REMENYYALQ TANEVKIICD INHHTTNHEI NTDPIRLHQI
IVNLINNAIK FTHQGEIHYG YIDQGDILRF YVSDTGIGID PKNFNDIFKE FNKLEPTNTK
FYKGAGLGLS IAKKLTELLG GHIWLESTPG VGSTFYFTLP NA
//
