ID A0A1M3KEP3_9CHLR Unreviewed; 1928 AA.
AC A0A1M3KEP3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BGO78_03550 {ECO:0000313|EMBL:OJX45973.1};
OS Chloroflexi bacterium 44-23.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895927 {ECO:0000313|EMBL:OJX45973.1, ECO:0000313|Proteomes:UP000184201};
RN [1] {ECO:0000313|EMBL:OJX45973.1, ECO:0000313|Proteomes:UP000184201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-23 {ECO:0000313|EMBL:OJX45973.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:OJX45973.1}.
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DR EMBL; MKUW01000007; OJX45973.1; -; Genomic_DNA.
DR STRING; 1895927.BGO78_03550; -.
DR Proteomes; UP000184201; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 6.
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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
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; PF13185; GAF_2; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 5.
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; SSF55781; GAF domain-like; 7.
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.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 852..884
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1701..1924
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 1545..1572
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1928 AA; 218009 MW; F0A195EC3FD20808 CRC64;
MNLSTDMLFG IFLIVLGVVL WLSVRFMLKS LFSERQTKIT GFSDLVNKAN DNLSEAIIQL
LPGGKILSIN RNAYSIFGVE EDPPVTLNSL AKNVEPESLF YQVCSQPDTV ELSIQAKNYQ
AMSYMLPERT LLFIRPIGNQ IERQETQRNT VTSELSAGLS HALTISLDPE LLVLNVLTQM
KEFILADQVE INLLNDEATH LIPFRIQTGK NGEKPFRAES KEKIGEGFSG KIIQSSEAVW
VRDLREYEST LHEIEEQTSD FKSFMGFPLI VDHEVLGTLE FYSNRLDGFK DNQRESVEKV
LPQITAALNN AILYRVEKHK AEELKSLAHL AQSASYSRDP YDIFERMLNT ISPLISVEII
GFLLFDESKL MLEAQRPFVG LPGPFVEIFK TTIIQGSQAE KIIRSHDVLL TENAEMDFHW
ITLGLDHIAR AASIRESVLI PLISGGEIFG FLMAGNHKAK PAAFSQMEMR LLLIVANQAA
PLIENMLLIQ QLNRKARLAE VLRKIAVFAN SGTSLEQIFS YSLEQLAELF NADCSALFLL
ENNASQLALQ NGSLFGCVGE SAFDSILPIQ DDQYPFTTTN SLKSIVIGRF DESEPIVPFY
QKLVDKWHLL SAMIVPLIIE DEGIGELWVG SGKANLFDFG DIPSLLPVAQ LLSEVIEQSK
HGDQSQVQWK KKVERLTVAA RVNREILNSQ DINTILQIIA QEEMHIVNAH AFSWVIIKQD
NSNNKSLMIL IEKGEKLTSE IRGSLATLIA QGKRVFGQDE DLLIGENRAT IFYPFELGNS
YFGGLFLYTN QKKGFTQADL DSVQSFISQV HQALITTFNA WEQQNTLEFM KSKMDLQKRL
FSISQRHGSE LAIQSVLDPI VAELMGFFTF REVSIYKFSR DDHGYKQLYC HTADDMNEIA
TNSDLIDWQT VELLKKPQYR RENFYQYQSS ELPDIFSRRC SEEENKPLDL LFNPIADFDT
NPAGLVCLGV DHGVQITDST LELLQVFIDQ IGLILENDAS YQVFDFETNE DFEKEKVTDA
TLETIQPVES LMESSRFQQL FGDSLFEDLL RMEDTKLFFS NFIKAIITKT EFDRVILFIE
NPDGSVCVQE SSSAEIDPNR LNALLGQRNP IQAVLNNWAP QTYPSHEIEG DWKRDPFFHE
LMADDYLFLP WQISSKKRAV LLMMRNGKIS PLSEKQIASF LEKLKLIGFL LDYRTEKEQQ
SIQLNEINDL NQFEQLTNSL NPEEILGQLL QTSFEQVPVA QAGWVGIWLE SDQALKPVLA
KGYRNSAALL RIRFTSAVWA IPSIVMEKRE VLQINDLNFA ANYPLLPEDL VHYQTATGGP
LPIGNLIAPL YFKDRNLGIL VLENFDGSSK FSNKDTGKVA AMAQQTSKTL HNAYLYRDSL
LISENLENQR DQLLLRLSII AATAGEKDLE TNITTALDQM SDAIHAEMAM LFNSDTKKLY
QCARDTNNKN AEATSLSLEL LQSIGESLIG NDETLILDEI YKNEKWLEKI SSDFPYLSLI
SIPLQYSGEN LAVLLFAHSE PFHFSKSDQQ LLESIAPQLS QLIVQTNLKD QLRQQQNRLA
EAEVEKIDIS SRSLAVLEAL KDGVIICNPS NEITFSNHVV EKILDLPYAS IQNLSIEELA
EKSKGSLDKW KNSIFQWANN AAFLNVGQQY SERIHLASQR IIAVQASPVL WNSQYLGAVT
MLRDMTVEAQ VDRIKTEFIA NVSHELRTPL TSIKGYIDIM LMGAAGEISD QQKRFLTVIK
NNSARLNVLV DDLLDVANIE NDRIRFDLRA VYLDKILSQL IKDYQSRSEQ ENKTLKFDVK
IPKNLRPVRA DAQRVKQILS ILLKNSYQYS QSGGKVIVRV SQSTSETQID IQDFGIGIKK
EYQDHIFERF FRGEDELVLA TSGTGLGLAV AKSLVEMQGG QIWFYSSGIK NEGSLFSFTI
PIYMQENG
//