ID A0A2P7THG4_9SPHI Unreviewed; 1352 AA.
AC A0A2P7THG4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7N43_25845 {ECO:0000313|EMBL:PSJ74092.1};
OS Sphingobacteriales bacterium UPWRP_1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ74092.1, ECO:0000313|Proteomes:UP000240367};
RN [1] {ECO:0000313|EMBL:PSJ74092.1, ECO:0000313|Proteomes:UP000240367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ74092.1,
RC ECO:0000313|Proteomes:UP000240367};
RA Tan S.M.;
RT "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT their spatial structures from highly complex communities.";
RL Submitted (MAR-2018) 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 -!- 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:PSJ74092.1}.
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DR EMBL; PXYE01000130; PSJ74092.1; -; Genomic_DNA.
DR Proteomes; UP000240367; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 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; 4.
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; 3.
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; SSF101898; NHL repeat; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000240367};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1352
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015167419"
FT DOMAIN 854..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1106..1221
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1254..1352
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1154
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1352 AA; 151722 MW; C00081442C731617 CRC64;
MGKHVWVWVV GCFAASYALA QNAYSPALTS QHYTAQHGLS DNYITALLQD RYGFMWIGTR
NGLNRFDGYD FVHYKNIQGS ANSLSNNYIT SLAEDLNGNI YIGTQGGLNR LNPVEGKIDR
FWHEPQQQNS IANNKIGDVF ADKEGIIWIG AYTVLDRFNP KTNTFTHFPT GIDPLQYSKE
LLSIEHITGF NGELILSVWG AGAYRFNVNT HTFLHIPYKT ETATKFAWPN CFTTDQTGKL
LTTDNITYVY NPTQKVFLPL NSPPKSNYDR VVNSVVIQAS SGQYYVGTMG SGIVRYDSRF
TSPQNLLVDA DTGNYYNNFI SVLSENTAGE LWIGTAGNGL FKHDLYAKPF GVLKKETNQP
NSLAADNIFS VSVMASGTIW IGTRSNGISI YNPIAHTFTH IQKSPVSKTG LNSNDIRSIF
EDSQGNVWIG TWGGGLNRID AISGKYTYFT LQPDDPLFML LDNFVTGVCE DSTGAIWVTT
TRGLSCIRQQ GSTAKVIKNY QYAEGKGQYA PSGLRLDAVF ADNNGQIWLG TETSGVSVFN
PCSETFTHLT YNPGDAHSLG GIKVNVIYED SRNRLWVGCA GGGLNLFLPN QKRFKHYTEQ
NGLPNDDIKG IMEDNKGNLW VTTSNGLSCF NPDAETFQNY LQQDGLPANQ FALQAIAKSP
KDGKIYAGTT KGLLHFYPES IEQNHLPPPV YVSAITLYQM RGGKTTGQTL SNTHTLKHLK
LRHTENTFTI QFSALNYRNS ALNQYAYQLQ GLNNGWVFLD TKREVTFSNL PVGKYRLRVK
AANNDGVWNQ NPTELAITIL PPWWQTGWAM LLWTCIVVAL LYSGWQYQLR RRLYEAEAKR
LRELDAFKTR LYDNITHEFR TPLTVILGMA DQLNPAANPQ QEAVNMIKRN AYNLLKLINQ
LLDFAKLQDK TLQLRPQHTD LVAFLQYITN SFRPYAQTQQ QTLQFTANTQ HAVTLLDTRL
LQHIMNNLLS NALKFTPHGG SIEVRLYLQP QLCQITVTDT GIGILPQDLP HIFKRFYQAN
TANARAQQGT GIGLAYVQEL VQLMQGYISV KSQPQQGTTF TLTLPFAETT QPIPPKPDAL
HELTEYPPLQ TTAQPANEDT NNHLPLVLLI EDNPDVITYL TLCLQTNYRL SIAFNGQTGI
EKALELIPNI IISDVMMPGK DGYEVCQTLK SDVRTSHIPI ILLTAKAAPP DKITGLRSGA
DDYLTKPFDQ EELLLKMERM TALQQRYLAR YAQSYLATPP NEQEEFEMED AFIQKITALL
ENNIADEDFA LPQLCQKIGM SRSQLFRKMK ALTNQSPSDF IRNYRLHAAK QLLLTTQLTV
SEIAYRVGYK DLAHFSKSFT EAFGINPSSF KK
//