ID A0A254NA78_9BURK Unreviewed; 1154 AA.
AC A0A254NA78;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CDO81_19205 {ECO:0000313|EMBL:OWR02328.1};
OS Roseateles puraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431059 {ECO:0000313|EMBL:OWR02328.1, ECO:0000313|Proteomes:UP000197446};
RN [1] {ECO:0000313|EMBL:OWR02328.1, ECO:0000313|Proteomes:UP000197446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 52769 {ECO:0000313|EMBL:OWR02328.1,
RC ECO:0000313|Proteomes:UP000197446};
RX PubMed=17978231; DOI=10.1099/ijs.0.65149-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Pelomonas aquatica sp. nov. and Pelomonas puraquae sp.
RT nov., isolated from industrial and haemodialysis water.";
RL Int. J. Syst. Evol. Microbiol. 57:2629-2635(2007).
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:OWR02328.1}.
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; NISI01000009; OWR02328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254NA78; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000197446; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWR02328.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000197446};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 490..709
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 765..878
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 887..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1034..1151
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 386..459
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 814
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 936
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1084
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1154 AA; 127413 MW; 3946A63F301CA128 CRC64;
MTDPRSGDSA QFRRILNRNL VLPLAMGLGS IVVFVGLLWH LIGLLNWVDH THRAVAKGHE
LATLSADQES GLRGFLLSGD DSFLTPYLLG QAKFLAELEG AERMMADNPA QVDKLRRVAA
LAKRWTVFAE TTIAMRRRGE SVEGIIRTQQ GKQLIDEMRR ELRSFNEMEL RLLRDRNEDA
QVGTWASVGS YIGLLLIVSG LIAWAGRRDI KALSSEYTNA LSSLADTARD NEARAWLRGA
QAELSAQLMG ERAQAGLATR TLAFLGERIG AVVSAAFLRG EDGRLRCVAA QGLAPADADA
RDADSGLLAQ VWRDGKTVRL AGVADDFLKV RTTLGDTLPQ DILLVPALHE GRVNAVFELG
FMQPPDERAR ALLEALQEML GAVFEAALAR QRLQASVEET RQLNEELQVQ QEELRTANEE
LGEQSRVLSE SQLNLEEQRA ELEQTNVQLA EQAEALTVRN AALAEAQAEL KARAFELQRA
SRYKSEFLAN MSHELRTPLN SALILSKLLM ENKPGNLNAE QLKFAGTIHS AGQDLLNLIN
DILDLSKVEA GKLDIAPRSL DLRALADSMQ RLFQPLAHDK QLRFEVKLAA GLPAAIVTDS
QRIEQILRNL LSNAIKFTEK GSVTLSIEPR GDHVAFVAAD TGIGIPAAHQ QRVFEAFHQG
DGALNRRYGG TGLGLSISRQ LAALLGGDLG LSSVESQGSV FTLTLPVHMP MPAQEPPQAA
PALPPVAARH HQPAVAPEQQ APLRSAPAFA DDREELVPDA APRRLALVVE DDPNFAGILY
DLAHEMQYRC LVANEAREAL ALASEHLPQA ILLDVRLPDG SGLAVLQRLK EDPRTRHIPV
HIIAGEDFRD VALPLGAVGT AIKPTTRDEL VEIFRKLERH GADEIRRLLL VEDDQRQRES
IAHLIGDDDI EVVAVSHGEE ALAQLDQQHF DCMIIDLKLP DMDGTELLAR MAERSVEKTP
PPVIVYTGRS LSREEEAQLN RYSRSIIIKG ARSPERLLDE VTLFLHKVES RLSGERQALL
RTARNRDQVF EGRKVLLVDD DARNIFALTS VLEQRGLTVE PARNGVEALE KLQAQDDIDI
VLMDVMMPVM DGLEATRRIR AESRWQKLPI IAITAKAMRD DQEQCRRAGA NDYLAKPIEV
DRLVSLLRVW LPTT
//
