ID A0A0U3LKE8_9BURK Unreviewed; 2219 AA.
AC A0A0U3LKE8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DES44_0313 {ECO:0000313|EMBL:REG21199.1}, RD2015_4126
GN {ECO:0000313|EMBL:ALV08575.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV08575.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV08575.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV08575.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG21199.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG21199.1,
RC ECO:0000313|Proteomes:UP000256283};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP013729; ALV08575.1; -; Genomic_DNA.
DR EMBL; QUMT01000001; REG21199.1; -; Genomic_DNA.
DR RefSeq; WP_058936515.1; NZ_QUMT01000001.1.
DR STRING; 76731.RD2015_4126; -.
DR KEGG; rdp:RD2015_4126; -.
DR PATRIC; fig|76731.3.peg.4226; -.
DR OrthoDB; 9146932at2; -.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; 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; cd00088; HPT; 3.
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; 3.
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; 3.
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; 3.
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; 3.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:REG21199.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000060699};
KW Transferase {ECO:0000313|EMBL:REG21199.1}.
FT DOMAIN 692..796
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1157..1256
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1346..1453
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1791..1927
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1929..2064
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2091..2208
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1404..1452
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1641..1668
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 739
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1203
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1393
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2141
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2219 AA; 237403 MW; 010D7174636A19D0 CRC64;
MDLSRESEFP ADLSPLAWVQ EELRRTLESV HKALRRVLRD TDARVSTLGG EGQPSPALQG
AAQQMHQAAG VLSVVSLPAA AQLLRAAEAT LFRLAENPAL VSVAEVEAVE RADFAVLAFI
AKTLAGGQPS SLALFPAYQT LQELNGAGRI HPADLWTQEF RWRDLAADTS VRALTPEQMR
APFEALLLKQ MRAPAPGQGQ LLSDLCAGLA LTQTQPHGRT LWLLAAAQFE AQSRGLLPVD
TLVKRLGSRL LAQLRAGRDA APSERLAKDL LFFAAAAKHP APGTAPRLEA VQVAYGLIEA
PSVDYRDDTL GKIDPTWVQA AKRRVATAKE SWGSAAEGET HRLGGLDEQF AGVAESLQKL
FPSGDVLGDT LRRAVVATLR SGRAPEPTLA MEIATAMLYL EAALEDEAFD QPEQAERVVN
LSRRIEAVAK GQAPEPLEAW MEELYRRVAD RQTLGSVVHE LRASLSEVER QCDEYFRDPT
KRDLLIPVPS QLQTMRGVFS VLGLSQAAQA TLRMRDQVDE LAQTEVDPAL PGPRAQFDRL
ANNLGALGFL IDMLSVQPHL AKRMFRFDDA SGLLQSLVGR ESEHHPVAEA ANEAPEQAPA
PQLLDQLQAT AAAVAQGDRP AEDLARDLER ISQEARAADD LNLAQAAQQA QQQLLSEGQE
NTAAESLQQF IEASAPVAPP AVPESAPIPQ EEAEVDQEML EIFLEEAGEV VTTARDALAV
LARDSSNREE LTTVRRAFHT LKGSSRMVGL NEFGEAGWAF EQLYNHRLSE HPQADADLLR
LSHEALDAFQ AWATAIGEKR PHGYSSVPFR AAADALRLEN RYAPLQISAA PVAAAAPVAA
AAAAAAAAAP VIVPADVPEL VEVPEIIEVA EVPEVVEVAE RPTAVETLDD RPLAPLEAAT
PVVADGLPSL ELPALDVPPL TADAAASAAS VTAAVDEPTL DLSLDFPSEA TAPARDVPEL
DVALDLPALS AEASLDVAPA VPELVDVPTL PVATADEAPL LDMPEGWPTD LDTEEVHATE
PMPLPIDDVV EAPALPADAT VSADSLDLDL LDLSSLDQPV AADASTAAAA ADADASTESV
DLHLDLNSEL LSSPSVQAEA PAAASAEEPI IEQAFAPVPA AAPVLSLVGG TAVDTDVPDE
DTDAAEDSDE GVKVIGHLRI SIALFNIFLN EADERSRRLQ VELTEWSLLP QSPLPQDAEP
LAHALAGSAA TVGFDDLSTL ARALEHALGR AQGHEVADPT LFQRGSDEIR RLLHQFAAGF
LKEVDGELLA QLQLFQPGAP LPDGALDSDE GLLAMSLDEV STAAHATEAP VPAYLAPTPA
VVPAADTSAD ASVNEFADDD FDFSLPDQIE PELMPIFEEE AEDLLRQLHA GLREWASQPQ
DASRASACMR VLHTFKGGAR LAGAMRLGEQ AHNLESQIER LMGDGAADHG QVTDLQDAAD
ALEYSFQNLQ RDWRNPAPVV PAPMVAPVAA PVVAPAPVEA PAAVQAVEPV ELLDVVEAVE
VPAVIETEAP VAAELPVEGS DAVVAPALET EEAPTAEAVA ETVTAPAAPV EAPAEAPVVQ
PQAQVPAVVA APVVPADIDI DWAHFSEVAD LGQPMESAPV APAAQVRVRG VLLERMAALS
GEVAIRRARL ESELGQMRTL LGDLDDNLER LRTQLRELEL QAEARIAARQ EAAQATGKDF
DPLEFDRYTR FQELTRMLAE SVNDVATVQR GLQRNVAAGE DELAGQSRLT RELQDDLLRT
RMVEFDSSLG ERLHRVVRQA ARESGKQAQL EVRGGGVELD RSVLERLTGA FEHLLRNSVV
HGIEPAAARE AAGKAPLGRI VLSLHQEGNE IQVRFTDDGA GLNLDRIRAR GESQGLIQPG
QALTDKQLME LIYEPGFSTA ESLTEMAGRG VGMDVVRSEV NTLGGYVITD STPGKGASFE
LRVPLTTALT QVVVLRYGDR KVAVPASLML SVQRLTADQV DKAYQDGFMQ VAGEQLPFYW
LGGLMNASER GIAQGRTLPV VLVHSAQQRL ALHVDEVLGN QEVVVKNLGP QLMQVPGLAG
ISLLASGDVA LIYNPVALAN RYGHAAQQRV HDLSAAAQVV VEKPSEPLPP LVMVVDDSLT
VRRVTQRMLE REGYRVLLAK DGLDAMERLS GDELPAVVLS DIEMPRMDGF DLVRNLRADA
RLRNLPVIMI TSRIAQKHRD YAQQLGVDDY LGKPYDEEHL LGLIGRYTAQ NLAGQAVVS
//
