ID D0YPU3_9ACTO Unreviewed; 810 AA.
AC D0YPU3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:EEZ92119.1};
GN ORFNames=HMPREF0578_1448 {ECO:0000313|EMBL:EEZ92119.1};
OS Mobiluncus mulieris 28-1.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=596328 {ECO:0000313|EMBL:EEZ92119.1, ECO:0000313|Proteomes:UP000005581};
RN [1] {ECO:0000313|EMBL:EEZ92119.1, ECO:0000313|Proteomes:UP000005581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-1 {ECO:0000313|EMBL:EEZ92119.1,
RC ECO:0000313|Proteomes:UP000005581};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) 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:EEZ92119.1}.
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; ADBR01000009; EEZ92119.1; -; Genomic_DNA.
DR RefSeq; WP_004013698.1; NZ_ADBR01000009.1.
DR AlphaFoldDB; D0YPU3; -.
DR eggNOG; COG0643; Bacteria.
DR Proteomes; UP000005581; Unassembled WGS sequence.
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; 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 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; 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};
KW Transferase {ECO:0000313|EMBL:EEZ92119.1}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 279..488
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 490..630
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 655..786
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 129..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 810 AA; 87906 MW; DDBA851D4E041E85 CRC64;
MGEMDEIVRE FLVESYENLD QLEQDMVSLE SEPGSKELLS SIFRTIHTIK GTSGFLAFNR
LEKLAHRGEN LLSELRDGVR EMDQETADVL LSMVDRIRAI MGSVEETGQE GDVDIDSVIA
QIEAIQGKTE SAAKPAAEQA PHETEETPAE VPFMTNVPDE KGETSMGEPT EVPFMTNVPD
EKGQTSMGAE APAAQAETKP EPAPAKPTQS AGAAVAAANS KKDTKSADHP TSDHGRSAAE
SSIRVDVDLL DVLMREVSEL VLVRNQIVRQ TDNMSDMNLV QSSQRLSIVA TELQEGIMKT
RMQPIEHLWS KMPRVVRDLA KQTGKKVKLV MIGGDTELDR SLLEAIKDPL THMVRNAVDH
GVESPEERKA AGKDPEGIVT MKAYHAGGQV VVDIIDDGAG IDPVAVANKA LDKGLVTSAQ
LQDMSDKDIF NMLFLPGFST AKKVSNISGR GVGTDVVKTS VEAIGGTVDV ESELGHGSTW
RMRIPLTLAI QPSLTVESHG ELYAIPQVSL LELVALDSSR KETSMEYVNA SPVYRLRGML
LPLIRLSHVL HPEETERRDE EANGVIAVLQ NDDQRFGLVV DKVINNEEIV VKPLSSKLKS
IGLYAGATLL GDGRVALILD IGAVARRSLT GASTQAAQKA QAAAEAAQAR ASDVIGQALV
VGIGDGRRVA IPLAAVTRLE HVNAEKVERV GGREVIQYRG QILPIVRLDR LLGVMDYEEP
KDLQVVVYNR GDRSVAMVVR EILDIVSDDK RKHSTVEDHG LLGSAVLKDR VTELLDVEQA
VRAADPTFFD EIDDFNTELE LGSRLDMVGA
//