ID D0S834_ACIJO Unreviewed; 1492 AA.
AC D0S834;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0016_00639 {ECO:0000313|EMBL:EEY97556.1};
OS Acinetobacter johnsonii SH046.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY97556.1, ECO:0000313|Proteomes:UP000012047};
RN [1] {ECO:0000313|Proteomes:UP000012047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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 ---------------------------------------------------------------------------
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; GG704964; EEY97556.1; -; Genomic_DNA.
DR RefSeq; WP_005399921.1; NZ_GG704964.1.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_9_0_6; -.
DR Proteomes; UP000012047; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
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:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 4.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 4.
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; 4.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 19..130
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 197..298
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 507..611
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 713..819
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 973..1206
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1208..1349
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1371..1487
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 914..948
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 66
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 241
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 554
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 760
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1420
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1492 AA; 166602 MW; 8BAA71EDD57148CD CRC64;
MKEILKHLVE TTTLPEDSYL DQDAEILEIF VEEIEEIFVD LDPLFEKWYA EPTHQETLLS
IRRHFHTLKG SGRMVGAKSA GETAWAVEDT LNRVISGAVP LTATVQKFAK TVFKLYQFKL
YPIFKAVQEI DLDLRPLVLI GQQLQQNQSL EPALEELLQL SNHLNSNDVV TGLELRDIEV
AESEPQVADA SEQDGQVHDV LEETLAIFIE EAEDHLATID HFLNADEAKV QDYNGLIRAL
HTLRGSSSMA QIEHVFNASS KVENLFKTLV QEEIVSTSKE ISLLTQYAEF VRDYLHVLGR
GTNEQLDVIY ATFTTAWDNY GFSIEDVADE LNPQGMVSKL IELNIDLLLD AEFEFDQRAK
VEYPDYIQHL GEQAKQLLEF TNNRAAQGIH DFTSELYAGY QALLEKPELL NVDYAYELFG
QAHQEFIHLF DTLAAGQRVI LTEEVHKVLN ELMAFVQQDV ESTSTTVIEP VAEAIVSGNT
LQPSLDLAQI SQQIASDHQY QQSNTANTDF DDDLLDIFLE EAEELLMGMD QDLNTWSKNG
NDTAALNNLM RYLHTLKGGA NMISAPFIGS IAHELESIYE RVIRQQIATT PQLISIIRLI
QDDVADRIQV IRTEKVDYPA TATIKVLHNI QSLVEGTTVT TTVSEPLVEA FVAAVEEPLS
NIDRTIEAEA AAVESATAIE EPSVVDNTDV TVVEQLDTPS PVQEEAVNAV EEAASLLSIV
EETFLEEAEE ILATTDGLLK QWTEQRSDRS VLLQLQRAAH SLKGGARMAE NEPVGAIAYE
LETTFEQFAV HNFSSNVYDP LLQTAFEWLK QAIFKRDFSN YDGLKNSLAS IDYVDVIAQL
PTRVTQIDLL NAVPSFEFVQ GDGTEPPAML GEWKETTHLD GGNEMIRISA DLVEKMIDLS
GENAINRSRI EMDLGQLGNT LNEMELAIKR LADQLRRMEG ELESQIIAKH GSENSRYADF
DPLEMDQYSS LNQLSKSLAE SASDLVDFKS TLAEKIRDAE GLLLQQSRIQ AEIQESLMRT
RLVPFSRMLP RLQRIVRQTA STLNRPTELV VHNTEGELDR TILERLVTPF EHMLRNAIDH
GIEDAEQRSA AKKSATGQIE LNISRQGTDV IVSFKDDGKG IDESTIKAKA LNLGLIKADQ
VLDKQEILQF IFHPGFSTAK EVTQISGRGV GLDVVQSEIK ALCGHVTVES EIGFGTTFII
RVPTTVAVSD ALMVKAGDQQ YAIPLAQIDR IVRIAPTALD HYFHSKDDQF KIDGVSYKLR
YLSEFLSNQP IPRLSNIGHS LPVLLIKGNS GQTIALLVDQ LIGSRAQIVV KPVGQQFASI
GAIAGATILG DGHVCLILDG QNIARQILST KRVTHAADHR DFGRHQDTRR LVMIVDDSVT
VRKVTSRLLE RQGFDIVTAK DGVDAMEQLE SVKPDLMLLD IEMPRMDGFE VTNLVRHHEI
HQNLPIIMIT SRTGEKHRER AFSLGVTHYM GKPFQEAELL ANIQQLLAEK QG
//
