ID K2BSC1_9BACT Unreviewed; 754 AA.
AC K2BSC1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Fragment;
GN ORFNames=ACD_46C00106G0001 {ECO:0000313|EMBL:EKD71753.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD71753.1};
RN [1] {ECO:0000313|EMBL:EKD71753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD71753.1}.
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DR EMBL; AMFJ01019526; EKD71753.1; -; Genomic_DNA.
DR AlphaFoldDB; K2BSC1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR007892; CHASE4.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF05228; CHASE4; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EKD71753.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EKD71753.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 378..429
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 513..752
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 333..378
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 754
FT /evidence="ECO:0000313|EMBL:EKD71753.1"
SQ SEQUENCE 754 AA; 85503 MW; 7FFB76DDB00FD325 CRC64;
MQLKTKVTLI ILLIWSILLV ATYFQGERIL SNSYLNLEQR KGLDNANEIT EVIDRMVNEV
SAMAAFWSIF DSAYEYMGDR NEEYIKTTVQ VTTLGKADLD MMLYYDIDGK LVYGLTVDPE
RSSEVPMPEG LEAYLDPKGK LVHQPNVDSS AKGIIAIPAG IFLVASHAIV KSDGTGPVRG
TEVLARRFTD ETIKKIADQT NLNLELYRLN KIEKQPELKN IYNDLIKSNQ PIINIEKNKN
KLNGYILLKD INNLPIAIIK LSEPLDVYKA GINTMYYFYM VFLAFGLIFI GIIIYLLRSL
IIKRIEILDN NIISISDKKQ FSLRVNEDGS DELTSVEKEM NKMLSVIDEY SQEKKKLINQ
VSNELDKANK FAKKLEEAEH LLSNTISFMP SLLVITNKDF KITHLNSIAE KFIGKNLDDV
KGKSIFELFP HINNYKNIFL KSYENQTKEM IDRVTFIMDG DKHHFNIIVY PFDISTGERG
LAIRIDDITD KENLENKLRQ NDKLSSVGVL TAGIAHEITH PIKSISVALN ALKISSSHLF
NLLDKYLSMN NQKIIHENTT GNYYTESNNE INKSIELIDE IVLAANQINE MVNNLRSFVR
MDEDMEKNVN IHDGINSILS LIKYKCQDRI KITKIFGNIP EIECVPGKIN QVFMNIITNA
IDAIPNDGEI TIKTYYQNDN IIISVKDNGV GISEENKSKI FDPSFTTKKS GIDVGLGLPI
SLGIIRELHG LIKFESQLGK GTEFIISLPI SKRK
//
