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Database: UniProt
Entry: A0A1Q7IC48_9CHLR
LinkDB: A0A1Q7IC48_9CHLR
Original site: A0A1Q7IC48_9CHLR 
ID   A0A1Q7IC48_9CHLR        Unreviewed;       977 AA.
AC   A0A1Q7IC48;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AUH89_02885 {ECO:0000313|EMBL:OLC61234.1};
OS   Ktedonobacter sp. 13_1_40CM_4_52_4.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805230 {ECO:0000313|EMBL:OLC61234.1, ECO:0000313|Proteomes:UP000186693};
RN   [1] {ECO:0000313|EMBL:OLC61234.1, ECO:0000313|Proteomes:UP000186693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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:OLC61234.1}.
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DR   EMBL; MNFP01000053; OLC61234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7IC48; -.
DR   Proteomes; UP000186693; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 3.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
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; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          398..435
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          477..529
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          735..967
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   977 AA;  108205 MW;  4F868D7D4C0D9F91 CRC64;
     MLGEHPSFTH EQEHQRLVTA LRESEILREL AELLASSLDL NNILTVLTRR TTEVCEVERC
     SVWLRDDTQD VFRPAAYYLS SQRIDREKIS SGDHLWRQGS VRFHDPDIFH LLQEKGMLVI
     NNLHDHPKVR NVADGFFVSS ILFVALKRED RILGMLTLDD PSFIRTFSPE QQQLASAIGQ
     QAALAIDNAR LYQQAQAERT RAERLIERAQ AIYQVALAVN SEENLSAVLQ IATHHLVSGL
     NADGGKIVLL EADMLHLADI AEQDQFHMAS SVETAFALRD LPHIHRAAST GSPLYVTAKQ
     ASVSEQQLFR KLSFSDVMVV PLITGSGHAK SSTPRTYTPP HTSQCIGFAF VNFQNPGYHP
     GKGQFAFAQD IAAQCALAVE KDRLLSDVHT AAALATERAN TLDAVFQAMT EGITVLNQDG
     EVLVRNNAAS RFLGIPINST ANLKALLQRF PTRTLHGQPL SEEEFPLSRA LKGERIHGER
     FVTVRGDGVE RVLEVNVTHM LDDSQRQIGL VSAFRDITEQ ARAEQRIRKA LETMLNVAEA
     FSGITEIEDI LQSVLGMTLS TLNCERGSVH LFDQNDQAFT ILLSSGFGDN ESEQEWLLEQ
     SLWLSPAENE YQGFRNQVLE GHATVINAEQ DDKQHQPINQ TMVLAAPITH NHRLLGLMIV
     DRFSSHTTGT APSKEERQSR PQEFSIWDMA VIEGIAQLAG LAIEQARWQE EAIKARTSEA
     AMREANALKD EFLAITAHEF RSPLTVILTH SQVGLRALRK GTEPQTIQRV NDSLTAIEEQ
     SHQLTNIVNT FLEVTQINRK QLVIKSEPID LAEIAEHVVA AHSATSAVHQ ISCQIAPSDH
     PYIVIGDDAR LKQVLANLLQ NAIKYSPFGG PITVSLCQHE SKEGDGRRTI DVCVEDSGIG
     IPQDALPRLF ERFYRGSNID GQSTRGIGLG LYIVAELIRM HGGTIRAESA GISGQGSRFI
     FSLPSSPLER ETAASGL
//
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