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Database: UniProt
Entry: A0A1J5FL72_9BACT
LinkDB: A0A1J5FL72_9BACT
Original site: A0A1J5FL72_9BACT 
ID   A0A1J5FL72_9BACT        Unreviewed;      1363 AA.
AC   A0A1J5FL72;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AUK34_05555 {ECO:0000313|EMBL:OIP60972.1};
OS   Ignavibacteria bacterium CG2_30_36_16.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1805221 {ECO:0000313|EMBL:OIP60972.1, ECO:0000313|Proteomes:UP000183261};
RN   [1] {ECO:0000313|EMBL:OIP60972.1, ECO:0000313|Proteomes:UP000183261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_36_16 {ECO:0000313|EMBL:OIP60972.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIP60972.1}.
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DR   EMBL; MNYQ01000089; OIP60972.1; -; Genomic_DNA.
DR   STRING; 1805221.AUK34_05555; -.
DR   Proteomes; UP000183261; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF12833; HTH_18; 1.
DR   Pfam; PF07494; Reg_prop; 3.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        787..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          840..1064
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1111..1226
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1258..1357
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1159
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1363 AA;  155789 MW;  FA86992A3DA0DFA3 CRC64;
     MIIMRFLFKI FTVLLIGLIF YPINIFGQSD EFSGYEFESF TVQDGLSSDI VYSLLQDKEG
     YIYVGTSTGL DRYDGIRFSK MPILSTTTTH KQNPIRCLAE DEEENIWIGS RLSGLIKYDK
     KNKYFTHFNQ NPYQNSISDN FIWAVICDTG NIIYAATRSG VDKFDTKKEL FSKLENESSV
     SGIFRFIKDD KNRIWARSSK GVLILYPKLM KLRLVDFSNL NMNLNSLGTI IEEPGSEGRV
     FWISANNLFV RIDIKSRETD KFDLLKLDPN LDKGRITNFL FDKNGDLWIG SRDGLGILKK
     NKNNFNYIPL VNNKFKAPGF SGNTISGILQ DKAGVIWVST ENGGINKYEQ RKIVVSPFDD
     SISKRYRDIL SVQLVANKLY LGVKQGLLEY DLTSKEQKVY DNLNSSPKKY SIRLTDIYQQ
     PSDPNILWIA SAEEGIHRFN IKTKLLEKFW RREMIKVLSY DCVMEDDNQN IWFGTTSSGI
     YKYFPKSDSI YSFSNNANKS APKGGITVLY NTKKGGIWIG TDGDGLHKYN SLKDDFINDI
     LSRKDSTLKN LIINAIKEDA NDNLWIGTSR GLVKLNVLTN EFKLYPLESK SRKAAVLSLE
     FDSSGNLWVS SMYNICRFDI RREMFSVYSP DKGQNTNYLP NCSQVLPDGK ILFGGYWNIS
     YIDPGQLNSH RPEIVITQIK LADQEPMIDP VLKDHFLVSL SYDENYFSIE FNALSFASPG
     RNKFIYMLEG YDKEWIESGM DRIARYTNVE PGEYIFEVKG SNCDGVWNEK GASFAVTILP
     PFYKTTWAYL FYVILLILFI YGIVKFFLYR DRLQNEAILK RKEAEQLQQL DQIKSRFFAN
     ISHELRTPLT LIIGPLESLI SKEKGNGNFQ LMYNQAKKLL NMINQLLDIS RLESGKMRLK
     ISKRDIIQHS QALISSFHPL AAKRKIKLSL ISPHTELKTY YDADKYEKIL INLLSNAFKF
     SPNEDEIIVT IESSNLTEFK GQPFPEGYIQ ITVKDNGSGI PETSAEKIFE RFYQLENQNV
     KKFGGTGLGL SIVKDFVELH GGLIYINTKV EKGAEFNFIL PLGKSTFKDA EFEQYFEESE
     SQTSTETLQN TVEIEITEPE KEISSNDAAK IILVIEDHEE VNDYIKNILS KYYKVIQSYD
     GESGLSAALK TVPDLIVSDI MMPGIDGYEV CKQLKTDEIT SHIPVILLTA KASLDSKIEG
     LETGADDYIT KPFSEEELKL RIKNLIATRE KLREKFAGQL NLNPTELSVT SADEKFLNRV
     KEVVEKNLPN PDFNVEDFSG KVGMSRMTLH RKLKAVTGLS AKELIQEMRL RRAAQLLEKN
     IGTIAEVAYE VGFKEPSYFT KCFQKRFNVL PSEYVKHEIS PII
//
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