ID A0A565BJ97_9BRAS Unreviewed; 1185 AA.
AC A0A565BJ97;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ANE_LOCUS11871 {ECO:0000313|EMBL:VVB01427.1};
OS Arabis nemorensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=586526 {ECO:0000313|EMBL:VVB01427.1, ECO:0000313|Proteomes:UP000489600};
RN [1] {ECO:0000313|EMBL:VVB01427.1, ECO:0000313|Proteomes:UP000489600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dittberner H.;
RL Submitted (JUL-2019) 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};
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DR EMBL; CABITT030000004; VVB01427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A565BJ97; -.
DR Proteomes; UP000489600; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF35; HISTIDINE KINASE 2; 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:UP000489600};
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 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..536
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 604..877
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 901..1022
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1045..1182
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 214..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 951
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1095
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1185 AA; 132076 MW; D730186FC38BB84C CRC64;
MSITCQLSNL TSKKANQSTG GVRKPLFFLI LCGLTTSVVI VLLIFSPLSK KEETSSCNGE
ARVLFRHKNV STSEIHALVS FFSDSDQVTS FECRKESTSG LRSNYCITCS LNMEKQSCHE
RQCFIPDGGV PWNLNPSGLE HSISPEACVS DNLEQSILQP KEHENHGEEP ENHGEELDWD
LSTYLRNTWW WLILGVLVCH KIFAFHSKAP TERKEKGSLQ EPLAQKQQRG QAPSKGAGRW
RKNILLLGVM AGVSVSIWWF WDTNEKIISI RRETLANMCD ERARVLQDQF NVSLNHVHAL
SILVSTFHHG KTPSAIDQKT FGEYTERTNF ERPLTSGVAY ALKVTHSDRE KFEKEHGWTI
KKMETEDQTL VQDCVPENFD PAPIQDEYAP VIFAQETVSH IISLDMMSGE EDRENILRAR
ASGKGVLTSP FKLLKSNHLG VVLTFAVYDT SLPPNATEEQ RVEATIGYLG ASYDMPSLVE
KLLQQLASKQ TIAVDVYDTT NASGLIKMYG SEIGDISEQH ISSLDFGDPS RSHEMHCRFK
HKLPIPWTAI TPSALVLIIT FLVGYIFNEA LIRIATVEED CQKMMELKAR AEAADVAKSQ
FLATVSHEIR TPMNGVLGML KMLMDTDLDA KQMDYAQTAH GSGKDLISLI NEVLDQAKIE
SGRLELENVP FDMRFVLDDV SSLLSGKANE KDIELAVYVS SQVPDVVVGD PSRFRQIITN
LVGNSIKFTQ DKGHIFISVH LADEVREPHN IEDAVLKKRL ALGCSESGET VSGFPAVNAW
GSWRNFKTFY STENHNSDKI KLLVTVEDTG VGIPLDAQGR IFTPFMQADS STSRTYGGTG
IGLSISKRLV ELMQGEMGFV SEPGIGSTFS FTVVFGKAET NLPVTKFERF DLAIQEFKGL
RALVIDSRNI RAEVTSYHLQ RLGISADIVS SLSMACTCVS KLRNLAMILI DKDAWNKKDF
AVLDELLNSS KESTTRPPKI LLLATSATPV ERSEMKSSGL IDEVVIKPLR MSVLICCLQE
TLVNGKKRQP NRKRRNLGHL LRDKRILVVD DNLVNRRVAE GALKKYGATV ACVESGKAAL
AMLKPPHNFD ACFMDLQMPE MDGFEATRRV RDLEREINKK IASGEASADM FSKVSSWHVP
ILAMTADVIQ ATNEECMKCG MDGYVSKPFE EETLYTAVAK FFEFG
//
