ID A0A1F8SJD5_9CHLR Unreviewed; 612 AA.
AC A0A1F8SJD5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-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=A2032_01100 {ECO:0000313|EMBL:OGO60020.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_49_13.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797667 {ECO:0000313|EMBL:OGO60020.1, ECO:0000313|Proteomes:UP000180309};
RN [1] {ECO:0000313|EMBL:OGO60020.1, ECO:0000313|Proteomes:UP000180309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGO60020.1}.
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DR EMBL; MGOI01000093; OGO60020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SJD5; -.
DR Proteomes; UP000180309; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..130
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 371..610
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 335..362
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 65
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 612 AA; 67402 MW; D2BCB0AA50B92394 CRC64;
MADHLLATRH HIVVLDDEPG ITRLCKRLLE RADFKVTTFT NPNDTLLAFK GEAATTPRPD
LLLVDIRMPD LDGFQVIDTA HKYFPDLAVV VMTGFGTVET AIEALRRGAD GLILKPFSTD
ELVQSVKRAL EQSQHKQDVL RLQALRPLFD VSESLFTETN PKRLRKLVLD AICGHLKCSY
AEFYQVEATS LKYDSGQAKS GPRLRLLASV HPPATDATAQ GGSGDKQSTS VRIETRPPTG
LLTEPIARKS GGLKAAMMIH LDSSTNSEVA DSQFQQVLAS SGLGSVISAP VSLKAGAIVS
GVLLAARNLR EPRFREADLE LLVVLARQAA VALENARLQA ELRDYIHQLE DSQRALIQAE
KMATAGRLTA SIAHEINNPL QAVQNCLHLA GRYELTEEQR QNYLGMALHE LDRLMQTVHR
MLDFYRPTAL DRNPLDVNSL LDRVISLVTK QMDDHNIRLH RNFAANLPPI LAVSDQIQQV
FLNLLLNAME AMPGSGDIFI VTTLAGEVKS TGKSASEKQV SQKEVEIYIE DTGQGIPMNE
RKHIFEPFVS TKDEGIGLGL AVSYGIVTAH GGSLDLIDYH TQLAVRFRSE FQYKSIGDGA
CFRVSLPISE HT
//
