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Database: UniProt
Entry: A0A101INA2_9CHLR
LinkDB: A0A101INA2_9CHLR
Original site: A0A101INA2_9CHLR 
ID   A0A101INA2_9CHLR        Unreviewed;      1081 AA.
AC   A0A101INA2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-JUN-2023, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=XE06_0006 {ECO:0000313|EMBL:KUK98248.1};
OS   Anaerolineaceae bacterium 46_22.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX   NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK98248.1, ECO:0000313|Proteomes:UP000054480};
RN   [1] {ECO:0000313|Proteomes:UP000054480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK98248.1}.
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DR   EMBL; LGHA01000001; KUK98248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101INA2; -.
DR   Proteomes; UP000054480; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 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; 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   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KUK98248.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:KUK98248.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          859..1075
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1081 AA;  119826 MW;  8006EC4F3E1A6849 CRC64;
     MSDIFAPLMP EYTIDLPKDP IALVAWVILF GLIVFFIIRL REKGAKIRRE SLIWMAILSV
     LVLVFTPFIG IPLEINSGNV FNQGKTFHIM FFAAVPWLAA GGIIGFIPAS LIAGVSGLLY
     AYLETHHIFT PLIFISFALF YTWGVRQNYH TAFYRYLRIP IISAFLALIM TTPLIFLTQI
     FISSGDYPFR IAIVLARMPA ILISYGGMLF SGSLICIILR ALFPNKWVSP AALMPSPSEK
     SVKSRFLLIT VPIMLGILIL FVGAVWHVNV NSSRSDLVGK LVNVSEVGAD AWTTFVDTGF
     LTLDEIGNAV QSTGGAGPDF QQLLSKKIEE ESFFDRLIIL SPDGEIISAY PGSGDVEPIE
     IPDAVFTDSD DFVKVAARSG RLDAELNFFE FLPQASDGMV RVLLGQTNIN QNPYARAFLS
     AFTSLKKFDA DGQILTRSGE ILFELDPDSL YGDLPEESFA TPTFYETGSP EGEPLMKYYA
     PIEGTAWAVF TQIPASVIYQ AAWQQSLPVL LTGIGILLVL LFAALYTWTP VLKDIRLISE
     EMKKLSDGRF EIQFTEPKSK GEVTQLFERF YLMTGTLGNR MKKHEDLLTL NEKMSFQNNL
     HDSLQAIMQS ALSRGISSVR LLLNDGVAVG KEGFYAGSQT DTYSHLDKEV AAIVRSQGEL
     VLRDSQIGKR LTFNKSLSYP LAIIGLPMSW QGDDQGVFWV AYHKKKSFTA EDIDFFHSLS
     SKAAAIIAKG ISFDNAVTLK THLEAILDNL TDGILLLNGE NQVVYHNHAA RLMLDLEHIT
     LLNAPITSLI SDRLLSEAIM AGENRGNDAR EFRLADNGVY KLEISSVDLA GQQQGKVVIF
     KDIRSAKKRE KLGSEFVTTV SHELRSPLTL IHGYAKLLRL TGNLNEQQDA YINNIINGVE
     ELKTLVINLL DIGRLESGKT LEIKRISAQG MAKNVVESMQ PFARQKNIHL EHVLPDFPVE
     IEGDEAFLAQ ALKNLLENAI KFTKMGGDVS LSVRKKEDTV VFAVKDTGIG IAPLDQRHLF
     EKFKRPSVNL GQESKGSGLG LAIVKSIAER HGGKVWFESQ LARGSIFYLE IPIKYDSRAG
     L
//
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