ID E0TEI3_PARBH Unreviewed; 996 AA.
AC E0TEI3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=PB2503_12064 {ECO:0000313|EMBL:ADM10455.1};
OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM10455.1, ECO:0000313|Proteomes:UP000001302};
RN [1] {ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RA Kang D.-M., Oh H.-M., Cho J.-C.;
RT "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM10455.1, ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RX PubMed=21037002; DOI=10.1128/JB.01205-10;
RA Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT the type species of the order "Parvularculales" in the class
RT Alphaproteobacteria.";
RL J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM10455.1; -; Genomic_DNA.
DR RefSeq; WP_013301429.1; NC_014414.1.
DR AlphaFoldDB; E0TEI3; -.
DR STRING; 314260.PB2503_12064; -.
DR KEGG; pbr:PB2503_12064; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000001302; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADM10455.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001302};
KW Transferase {ECO:0000313|EMBL:ADM10455.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 627..850
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 878..994
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 929
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 996 AA; 107134 MW; FB12D3CE7B3BF212 CRC64;
MSLPLFRRKK ARVDESEEGR NETASGSLTD QFGGSPFFEA ELVDEFESEI ARGGDGELTD
EEDILDVVEA MPPDSTSQKD PRLLGAPPAP PVEADMDATA ADDAGETEGE TENEGHRPAD
APDPHIAASE AVDQHDPHAD YQRPYSSTPV HDNLASGEPL IEKLTPVALW AAVALVFASL
IYGVVAGGVN VPTLAIFATG VGIFAAILGT AAVTGAYSPL LLSGMLLNRA TASQDEALGL
AGRNVLAGLG LAENLIDADV DARLMTTRDG VVVYANQQYL KLAKAAGVTT TTGLPPRIDR
LFAQAAGESS KMFRLARAAR SGLEADEVIT QTMGTTAEQT VVRRRFEVSV RPMSDKGKHI
AWRLKELPVE SALETFRRAY DDYPRPVIAL EKSGNVPWIN KAGVTFLGPR SIRDAHLSEF
VLGEAKEIIS SLWDETGEEL ESRVRTRKND QSQSVAIVFT PFTKAGLGEG FVCVEMLPRE
LTDAHTATSD AAGDVTEAPI GVALVEGDVG TDAKLASVNR LFSSYFGAKP GMRLNETLSS
EAVRDLQAAL KVKSAQKPLT QTIDMTIGEG ATAINLKVLA RPIKRRRGAY GPRQTVLYAL
DVSFQKRMEE DYAHDKRLKA IGKIAGSVAH DFNNFLQAIL GATELMMRRH PAGDPSYQDL
VEIKENSQRA RNLTSNLLAF SRKQTLQAEI LSVSDVLSEF QPFVQRYVTE KVKVSLEHGR
NVGCFKVDRA QLELAIMNLA VNARDAMEKG GTLTISSKRV KAEDVAGYGY AVLDEIDHIL
IEVSDTGPGV PEEIADKIFE PFFTTKGEGK GTGLGLSTVH GIIGQLGGRI FLKNRPGEGA
TFLIFLPALS ADVVPEQPQI DEASAAASRV VDLTGKGRIL IVEDETSVRN VVVRALGSCG
YDIVEAADGD EALEIIEDDD GHFDVILSDI MMPEMDGPTL IQEAGDKIAG VKVIFMSGYA
ETAMRDKLGE IKGAGYLQKP FTLKKVAAVV KEAMTS
//
