ID A0A0P7X2N1_9BACT Unreviewed; 817 AA.
AC A0A0P7X2N1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HLUCCA01_08910 {ECO:0000313|EMBL:KPP94767.1};
OS Bacteroidetes bacterium HLUCCA01.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1666909 {ECO:0000313|EMBL:KPP94767.1, ECO:0000313|Proteomes:UP000050310};
RN [1] {ECO:0000313|EMBL:KPP94767.1, ECO:0000313|Proteomes:UP000050310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA01 {ECO:0000313|EMBL:KPP94767.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) 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:KPP94767.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIHN01000021; KPP94767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7X2N1; -.
DR STRING; 1666909.HLUCCA01_08910; -.
DR Proteomes; UP000050310; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 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; SM00086; PAC; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPP94767.1};
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 202..253
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 448..669
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 699..815
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 750
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 817 AA; 92111 MW; E109A610E3900712 CRC64;
MSLYSSFLEQ APFGFMLLEP LYENEVVTDA RFLSCNRSML DIFGKSPDTD LTGQRFRAMI
PAIDDKAKVD FFGLCTQVLR DKKISKSTEY SRYTHRWLKT DIVPIDNGTL AVSIYDVTDQ
YGELSEARDM LARTGRIARV GGWEKDLVNN RDYWSEVTRE IHEVPPDFDA NSVPRFHFYD
RGENHAALVQ AVNHSYATGE PFDVQTRIIT ARGNKRWVRV LGYPTLKDGK PVYVHGIFQD
ITEQKEQQLL LERNGAFQQL IAETSASLIN VTNENFDAKV DSILQRFGRF FNADRSYLFR
YNEDCTVATN THEWVEDGIE PQIHNLQDLS AEYIPWWTSK LTQNYPVFFH DIDTMPAEAS
MEYQILKEQD IKSILVVPIF LRGITLGFFG FDAVRDYRTW FEDDISKLRL VATMLSDAID
KVRIDRELIE AKDRAVAASK AKSQFLANMS HEIRTPLNGV IGYTELLFDT TLNERQYRYL
ETVKISAQSL LNIVNDILDF SKIEAGKLDL DPVPADVHEL ADKALLMFKY QASRKQLDLV
LDVDETTDFN VVVDPHRLNQ VILNLVSNAV KFTDEGSVTL ALKLDELPSG MGRLRVSVHD
TGIGIAPQAR ENLFKAFSQA DGSTTRRFGG TGLGLVISNL LVGKMGGEIG IRSEPGKGSE
FFFSIDVPLV RGHRHSVHKK DMVKTRTGST GLSFIPSPTI LIAEDIPLNA NLIRLVLNKL
IPDAHILMAE NGKIAVDIAM NNPVDVILMD VHMPEMDGLE ATRTLRSRNH DAVIIALTAG
VVAEDKERCM DAGMDDFLAK PVQQDVVAKM LYKYIGA
//
