ID A0A6D2JBQ0_9BRAS Unreviewed; 1028 AA.
AC A0A6D2JBQ0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MERR_LOCUS21675 {ECO:0000313|EMBL:CAA7034440.1};
OS Microthlaspi erraticum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Coluteocarpeae; Microthlaspi.
OX NCBI_TaxID=1685480 {ECO:0000313|EMBL:CAA7034440.1, ECO:0000313|Proteomes:UP000467841};
RN [1] {ECO:0000313|EMBL:CAA7034440.1, ECO:0000313|Proteomes:UP000467841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mishra B.;
RL Submitted (JAN-2020) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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; CACVBM020001147; CAA7034440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6D2JBQ0; -.
DR Proteomes; UP000467841; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.250.1190; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR000836; PRibTrfase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF73; HISTIDINE KINASE 3; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000467841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..389
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 457..721
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 747..866
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 892..1020
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 942
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1028 AA; 115325 MW; A061E16850BC7946 CRC64;
MSLFHVLGFG VKIGQLLWML CCWFVSWFID GGIEDKPGLL IGSVGDPSPP EKTKMTTTMK
KKSKLCFWSK IFKIPSFSHH FLGSVRFGKT WWRKVVVAWV VFWVLVSFWT FWYFSSQAME
KRKETLASMC DERARMLQDQ FNVSMNHVQA MSILISTFHH GKIPSAIDQR TFSEYTDRTS
FERPLTSGVA YAMRVLHSER EEFERQQGWT IRRMDSLEQK PVHKDDYDPE ALEPSPVQEE
YAPVIFAQDT VSHVVSLDML SGKEDRENVL RARKSGKGVL TAPFPLIKTN RLGVILTFAV
YKRDLPSNAT PRERIEATNG YLGGVFDIES LVENLLHQLA SKQTILVNVY DTTNHSQPIS
MYGSNVSADG LELISPLNFG DPFRKHEMRC RFKQKPPWPV LSMVTSFGIL VIALLVAHIF
HATVSRINKV EEDCNKMERL KKKAEAADVA KSQFLATVSH EIRTPMNGVL GMLHMLMDTE
LDVTQQDYVR TAQASGKALV SLINEVLDQA KIESGKLELE EVRFDLRGIL DDVLSLFSGK
SQQKGVELAV YISDRVPEML IGDPGRFRQI LTNLMGNSIK FTEKGHIFVT VHLVEELLDS
IDAETASSSP ESTLSGLPVA ERKRSWENFK AFSSSGHQSF PSDINLIVSV EDTGVGIPLE
AQSRIFTPFM QVGPSISRTH GGTGIGLSIS KCLVGLMKGE IGFSSTPKVG STFTFTAVFA
NGMHTAERKS DPQSNNQPMF SEFQGMKAVV VDHRPARAQV SWYHFQRLGI RVEVVPRVDQ
ALRFMKNGTT AVNMILIEQE IWNREADAFI KKLQKDPLVR SPKLILLANS IETSVSDTLS
SGVDPPMVIV KPLRASMLAA TLQRGLGIGN RETPQHRGPP ALVLRNLLLG RKILIVDDNN
VNLRVAAGAL KKYGADVVCS ESGVKAISLL KPPHEFDACF MDIQMPEMDG FEATRRIREM
EEEMNKRTDS SKARWHLPVL AMTADVIQAT HEECLKCGMD GYVSKPFEAE QLYREVSRFF
NSPSDTES
//
