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Database: UniProt
Entry: K2C6K0_9BACT
LinkDB: K2C6K0_9BACT
Original site: K2C6K0_9BACT 
ID   K2C6K0_9BACT            Unreviewed;       478 AA.
AC   K2C6K0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 43.
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_34C00564G0001 {ECO:0000313|EMBL:EKD88400.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD88400.1};
RN   [1] {ECO:0000313|EMBL:EKD88400.1}
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:EKD88400.1}.
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DR   EMBL; AMFJ01012907; EKD88400.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2C6K0; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 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; 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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EKD88400.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:EKD88400.1}.
FT   DOMAIN          137..207
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          271..478
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   NON_TER         478
FT                   /evidence="ECO:0000313|EMBL:EKD88400.1"
SQ   SEQUENCE   478 AA;  52511 MW;  5DBBD45F77BAFC60 CRC64;
     MSMNTNTSAE SEFSKIENAV LRAKKEWEAT FDRIPDLLVL TDADGIILRC NRSTIDKLDT
     TYHKILGQPI SSFFADAKAP HVEVDDRVGA EVQIIGVSDW FKLTSCQVPL SGNDNSLLFI
     FQDITRQKHD ENEILKQKEF FESLFQYNPV AVVILDLEGK ISSINPAFEV LFGYAEGEVI
     GQQLDPLVAP ETLQEAADLT KTVLDGGAVR GLANRQRKDG TKVDVEFAGV PVIVEGKKQG
     ILAIYYNVSE LVEAKRLAEQ ADRAKSEFLA NMSHEIRTPM NGIMGMLELL LDTSLNSEQR
     DYVSTARDSA EALLGILNDV LDFSKIEAGQ LTIDAIEYDL RSTVEGVAHT LVSRAENKGI
     ELACLIDKDV PSRVLGDAGR LRQVLINLVG NAIKFTSEGE VVIRVMMQSK TEKTSTLRFL
     VSDTGIGIPL DRQKAVFERF VQADSSSTRK YGGTGLGLTI SAQLTKMMGG DIGLESEP
//
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