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Database: UniProt
Entry: D0YPU3_9ACTO
LinkDB: D0YPU3_9ACTO
Original site: D0YPU3_9ACTO 
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}.
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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
//
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