ID A0A3T1AQ69_9ACTN Unreviewed; 787 AA.
AC A0A3T1AQ69;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-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=ACTI_16690 {ECO:0000313|EMBL:BBH64984.1};
OS Actinoplanes sp. OR16.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=946334 {ECO:0000313|EMBL:BBH64984.1, ECO:0000313|Proteomes:UP000282692};
RN [1] {ECO:0000313|EMBL:BBH64984.1, ECO:0000313|Proteomes:UP000282692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:BBH64984.1,
RC ECO:0000313|Proteomes:UP000282692};
RA Kasai D.;
RT "Complete genome sequence of natural rubber degrading Actinoplanes sp.
RT strain OR16 isolated form botanical garden in Japan.";
RL Submitted (DEC-2018) 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; AP019371; BBH64984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1AQ69; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000282692; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 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; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
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; IPR037257; T2SS_E_N_sf.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 2.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 2.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 242..486
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 488..622
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 642..773
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 133..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 787 AA; 84901 MW; 1A533B47932AA72D CRC64;
MEDLGEIVGE FLMESHENLD QIDRDLVALE QEPDSRDLIS RIFRAIHTIK GTSGFLAFTR
LEKLAHAGES LLSRLRDGVQ PVTPETITVL LVTIDGVRNL LSSIEENNTE EGIDIDSTIE
RIHAQMNAPA AAAPAAAAPA AEAPAEAAPA AEGEAPVPLD ETPKRPAPEP VAEQRQPLGQ
ILVEAGAAQQ NDVTSALQQQ IEGDERKLGT ILLEEGKAAP AAVSEALQTQ APKRSIADSA
IRVDVDLLDT LMNMVGELVL ARNQLVRGVM EIGDATLVRS AQRLGMITSE LQEGIMKTRM
QPIEHIWSKL PRVVRDLSNS LGKQVQLVME GKETELDRSL LEAVKDPLTH LVRNAVDHGI
EDPERRAASG KGPEGTLTLR AYHEGGHVAV EVADDGAGLN VERIAQKAVE NGLLRPEQIP
SMDKRDIMAM VFQPGFSTAA KVTNVSGRGV GMDVVKTNIE NIGGAVSVDS TPGEGTVWRL
TIPLTLAIIQ ALTVDCGDQR YVVPQVAVLE LVFIDGNATK VEYASGAPVY RLRGKLLPLV
RLDRALGFEV GGDQGVYVMV LQADGRRFGL VVDRVLNTEE VVVKALNTRL KDIGLYSGAT
ILGDGKVGLI LDVPALARRS HLAADSEREN VVEKRGQAAG GTERLLVTAV GERRVAIPLD
TVTRLEEFPR DRLEHAGSRE VVQYRGQILP LVRLSHLLGA YGEELEGDTV SVVVYSEGGK
SVALVVDRIV DIAENSTTAR REAEEDGLVG TAVIQQRVTE LLDVRRAILA ADPNFYNDSM
DDMLVEA
//
