ID A0A2E7P1M1_9BURK Unreviewed; 770 AA.
AC A0A2E7P1M1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CME87_09105 {ECO:0000313|EMBL:MBO15629.1};
OS Herbaspirillum sp.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO15629.1, ECO:0000313|Proteomes:UP000226028};
RN [1] {ECO:0000313|Proteomes:UP000226028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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:MBO15629.1}.
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DR EMBL; PBPP01000060; MBO15629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E7P1M1; -.
DR Proteomes; UP000226028; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:MBO15629.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:MBO15629.1}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 349..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 489..623
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 648..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 154..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 697
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 770 AA; 83222 MW; 9E131E286A9C222B CRC64;
MSTPDLSQMS MLDLFRFEAE SQIAQLNTSL LALEQQPTAA EHLEACMRAG HSLKGAARIV
GLETAVKVAH VLEDCFVLAQ QGKLRLEKKH IDVLLRGADL LGRIASPPDG DETWVDHAGS
AEVQAFLQAL PAVISGADAD PWPAPSAALQ EAFAAEAAPQ PPAPAPSALV TEPPQSGASA
PIVNQTAAAR AVRVSADSLD RLLSLTGESL VESRRLKPFS ASMLRMKRVQ REAVQALDLL
QQKLAASQLD EFAQTTLAEL RALMQTNQQL LGEQLIALDA FDRRSVNLSQ QLYDEALACR
MRPFADGTAG FARMVRDVGN ALGKSVRLDI SGTATQIDRD ILEKLEAPLG HLLRNAVDHG
IEDGSTRRAA GKPEQGVVRL EARHSAGMLL IEVADDGAGI DLDALRRTVV ARGLATQEIA
ERLSDAELLD FLLLPSFSLR ETVTEISGRG VGLDVVADML KQVRGTIRIT TRPGQGSRFL
LQLPLTLSVI RSLLVEIAGE PYAFPLAYVN RTLRLPAEAL QTLEGYQHFS HGGRQVGLVS
AHQVLQRGQW RVRDGSVCVV VIGEEEHSYG IAVDAFLGER MLVVQPLDAR LGKIPDILAG
ALMEDGAPLL ILDVADLLRT VEKLTASGRL QTVDADPAGA AAVAVRKKVL VVDDSLTVRE
LERKLLTNRG YQVTVAVDGM DGWNAVRAEH FDLVITDIDM PRMDGIELVT LIRGAPQLQA
LPVMIVSYKD REEDRQRGLA AGADHYFTKS SFHDESLLQA VMDLIGEATT
//
