ID A0A2S5T9Q8_9BURK Unreviewed; 1286 AA.
AC A0A2S5T9Q8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C1702_01660 {ECO:0000313|EMBL:PPE71723.1};
OS Caldimonas thermodepolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=215580 {ECO:0000313|EMBL:PPE71723.1, ECO:0000313|Proteomes:UP000239406};
RN [1] {ECO:0000313|EMBL:PPE71723.1, ECO:0000313|Proteomes:UP000239406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15344 {ECO:0000313|EMBL:PPE71723.1,
RC ECO:0000313|Proteomes:UP000239406};
RA Tang B.;
RT "Reclassifiation of [Polyangium] brachysporum DSM 7029 as Guopingzhaonella
RT breviflexa gen. nov., sp. nov., a member of the family Comamonadaceae.";
RL Submitted (FEB-2018) 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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:PPE71723.1}.
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; PSNY01000001; PPE71723.1; -; Genomic_DNA.
DR Proteomes; UP000239406; Unassembled WGS sequence.
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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
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; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000239406}.
FT DOMAIN 224..295
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..350
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 423..477
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 478..542
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 622..846
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 866..987
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1004..1127
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1188..1281
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1134..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 920
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1053
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1227
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1286 AA; 142141 MW; B3B800F50B60D5EF CRC64;
MQLIAAGLLA AAGWLWAWRG QGLPAAGSLP LLVAAAAWAW RVRTSPAPPP ALAARHAALE
AVVEAVNQAR TLGAALEAVG QALARYMGAQ GHAVLQVADW NGQTGVVFPW DERGNGHESH
LDLERLAVVR ADDGLAGSAI ARHAVAASPG PLPGHPWRAP GACGGVAVPV WSDDEPVAVV
EWYGLQRSTD DVDLQQLLAT AMGQLSVLAR REVARSGMVL HQERLRRIAM VAARVPSGVI
IADERGRIEW VNEACSSITG LPAEQLIGRE CWALMSDPQT AQALRGAIAE AKDFRLEFQG
RRLLDDGTVA PYWAEIDVAY VLDEQEARFV YLAVLSDVTE RQLKAEQLEA ERAHLDELIE
HLPVSLYVME PGQLRLLAVN QHAEREFAVQ REALLGLPAE QALGRKLTAL ILPAIRHALD
GGEPIEDEFV WTTRQRGERV LNARCIALRH PDGTPRAVIV IARDLTERRR AEGALMESEA
RFREFADAVD DHLFITTPDR SSFLYVSDRL QAFWGVTPDE HARNPRAYLE HVPPEDRPLL
DECEQRERQL LPVDFVHRLR HPTRGLRWLR TRTRARQLPG GGIRVYGLCT DITEEHEREE
ELQRARDAAE AASRAKSQFL ANMSHEIRTP MNGILGMTEL LLGTALSEKQ RRFAQAVYRS
GESLLEIIND ILDFSKIEAG KLELAPTAFS LRAVVEDTLE LMAPRAHEKA LELNFREQPG
LPPVLHGDPL RLRQVLTNLV ANAIKFTERG EVVVDVQQVP GVPVPPGQVM LEFTVRDTGI
GIAPEVLPRL FSAFTQAHGG MARRYGGTGL GLAISKQLVE MMGGEIGVTS MPGQGSRFTF
RVPLGIVAGA GEGLVEEDAQ QMPALRVLVV EDNETNRTVL ENMLGAWGMR VALARDGVDA
LELLEREREL GGQFDLALVD MSMPRMNGVQ FARAVREQPH WRHLKLMLLS SVSSPDDVRV
AHDVGFQRFV AKPVRKVELR QAILGLSAPP ARQREQPLPR LDRHVLVIED NPVNQEVIHQ
MLRRLGCRTH LAHSGLEGLR ALCEHRFDLV LMDIQMPGMD GVETLRWFRR GSGGRFEFRT
PPDTPVLAVT ANALGGDEER FLAHGFNDYL SKPFRQSQLL AVLTHWLKPA MEDADGRAGA
PDAQPTMTAV GTTAARTDDR EPKMIEPDPQ VFDADAVARL RELDPQGENQ LLLRLFRTFH
TSLHRLVPQM EEAHELNDLA TIRLAAHTLK SSSASVGAMR LSALCAEIES LIRSGQPGPY
DRLMETIRQE ADRVLGSLRT LLGSDR
//
