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Database: UniProt
Entry: K1YTF6_9BACT
LinkDB: K1YTF6_9BACT
Original site: K1YTF6_9BACT 
ID   K1YTF6_9BACT            Unreviewed;       735 AA.
AC   K1YTF6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
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_75C01766G0001 {ECO:0000313|EMBL:EKD35823.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD35823.1};
RN   [1] {ECO:0000313|EMBL:EKD35823.1}
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:EKD35823.1}.
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DR   EMBL; AMFJ01032435; EKD35823.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1YTF6; -.
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   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKD35823.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..180
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          195..419
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          438..559
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          588..707
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          711..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         491
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         639
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKD35823.1"
FT   NON_TER         735
FT                   /evidence="ECO:0000313|EMBL:EKD35823.1"
SQ   SEQUENCE   735 AA;  80399 MW;  7E527337452B3784 CRC64;
     QLTRNFHRYR SIAVAVTFGL ILTCALFSAI SIVSLLGFRN FHHALTHISG KLAEEVRPAG
     TTAGNHGESE RNVGEKVGLR SADSAGGLPE LARQAEKLAK HAEQHIKILA TLFVLSLLLA
     LAFFFYFRGN LIARLTRLNQ TVLAMVEGQN RQIVDTGYDE ISAIASSVNF FSAELYKAKA
     AAERSAITKS QFLAHMSHEI RTPMNAILGF SDLALQTDNP SDHFDYLGKI NTASYSLLGI
     INAILDLSKI EAGKLTVENV DFDLRELLEK LATLISLRCE ESGIEFYFNI APETPFALRG
     DALRLSQVLT NLITNAFKFT ESGYIVLHIS PDPGRVIGSD RVILRFSVQD TGTGITKEQE
     ENLFQPFTQA DSSITRKFGG TGLGLTICKS LVAIMNGSIW LERNDTPGST FCFTVPFARK
     EGHDRDFYSA PGMVAGKRMI VMSERPQKAS ELSYQLAAFG IEVCQALTVQ EVVSALGEQL
     LQNPYEIVIV DCEIYSQRWL EIPGKIKAAA AAAVAPALIL TGMQRLSTHF SAHNINGCDY
     FLSKPITPAR LLDAILTVLG ADNPDPVASL DKRSAAPLPS LDHLLGNRVL LAEDNKINQQ
     ITLGFLDFAG LATTIVQNGA EAVELLEREG TSFDLVLMDI QMPVMDGYSA TEAIRKMAAP
     TGKIPIIALT AHAMQEEKQK CLDRGMNDYI TKPINPEQLF ATLGRYLPCR PPALRPPAKP
     QEPESLPEEQ AAGRH
//
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