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
//