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
//