ID A0A0U3F4P9_9BURK Unreviewed; 1069 AA.
AC A0A0U3F4P9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AT984_20535 {ECO:0000313|EMBL:ALT79224.1};
OS Paucibacter sp. KCTC 42545.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT79224.1, ECO:0000313|Proteomes:UP000056576};
RN [1] {ECO:0000313|EMBL:ALT79224.1, ECO:0000313|Proteomes:UP000056576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT79224.1,
RC ECO:0000313|Proteomes:UP000056576};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Paucibacter sp. KCTC 42545.";
RL Submitted (DEC-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; CP013692; ALT79224.1; -; Genomic_DNA.
DR RefSeq; WP_058721696.1; NZ_CP013692.1.
DR AlphaFoldDB; A0A0U3F4P9; -.
DR STRING; 1768242.AT984_20535; -.
DR KEGG; pkt:AT984_20535; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000056576; Chromosome.
DR GO; GO:0016020; C:membrane; 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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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 Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00091; PAS; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000056576};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..362
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 381..425
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 454..506
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 524..740
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 764..881
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 962..1063
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 906..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 917..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 816
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1004
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1069 AA; 116164 MW; EB9A0D2E8A894C06 CRC64;
MQAPPPDPSS MPKLELGGAK AWQRRQQTLR DFELRLEDRV KRSASVFLLL VVLGVLAFLA
AKLMLTELSW AARLQRMAAG MLYLGAALVS LGLLHRVSVR AGTLFFCWSA LALQLGAAAY
YGTGLYSSGM ATLVALLAVV GLLLGPGAAV RGTVLTVLGI LGLWFMQEQD LLGKVEPNTF
PPLASFAVVL VMCALVVGWL ALRHGTLFRE VMLSLDSSRQ LLADTLRAQQ TAVEELRASD
DRMRVLLDHS LSCTLILDGE TGQLRFANAQ TLLKHGCERI SELDASLFFP GDPFSREQGL
AHMREVLSQG AQYFEWQTRH RDGTPIWWDI KLERLHVCGE TIVVAFAHDI TERLRAENEL
RVQRARLEEQ VNERTHELIS EKQRLQDIIE ALPITLSIRD CQGRYTLLNR SFELATGHGR
EQVLGLSARH FMPAEIAAEI ADTDAQLIAG KASMTTERQI MHPVDGMHDY LVTTVPLLDA
RKRTYALLNL GTDVTSLKRL QRELSLAKDE AEHLARVKSE FLANMSHEIR TPLNAVLGLA
QLGVGRAGDP AAARSGFERI TRSGRHLLSV INDILDYSKV ESGKLEIDPL PCNLSHLARE
VLDLVAERAE AKHLRLRLDY EVAEDWVAID ALRVTQILVN LLANAIKFTD KGRVTLGVTQ
AADGLRLSVT DTGVGIAPEQ QARIFKAFEQ ADSSVTRQFG GTGLGLSISS RLAEAMGGEI
TVSSEVGKGS CFTLRLPCVV VSGEAHAQPL INAAVPPDLL RGLRILIVDD VDINREILQD
LLCLAGAEVM SADSGEQALA RLGEAGPEGY DLVLMDVQMP EMDGYETTRR LHQMAPRLRV
IALTAHALPE ERRKCVAAGM LGHVTKPIDQ AELMQALLEH SHDLPRRAAD AISPSQLVPL
DAAPDVQPRA PAMAPASPPT SVSTESQDSA VPTAPTVPTA PAARTSFWPD LPGCDFEAAL
TRCAGRQELL AKLLGTFAKQ YAQYQSVFEE ARISGLPALA SAAHRLKGLS GNLGLSRLAQ
SAESLETAAG GRGDPAQVPA ALTALIREIA PMVSSIAAWH EAYTARIKA
//
