ID A0A1E7X669_9BURK Unreviewed; 983 AA.
AC A0A1E7X669;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_2 {ECO:0000313|EMBL:OFA08529.1};
GN ORFNames=DUPY_06580 {ECO:0000313|EMBL:OFA08529.1};
OS Duganella phyllosphaerae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=762836 {ECO:0000313|EMBL:OFA08529.1, ECO:0000313|Proteomes:UP000175989};
RN [1] {ECO:0000313|Proteomes:UP000175989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T54 {ECO:0000313|Proteomes:UP000175989};
RX PubMed=27833590;
RA Haack F.S., Poehlein A., Kroger C., Voigt C.A., Piepenbring M., Bode H.B.,
RA Daniel R., Schafer W., Streit W.R.;
RT "Molecular Keys to the Janthinobacterium and Duganella spp. Interaction
RT with the Plant Pathogen Fusarium graminearum.";
RL Front. Microbiol. 7:1668-1668(2016).
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:OFA08529.1}.
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DR EMBL; LROM01000047; OFA08529.1; -; Genomic_DNA.
DR RefSeq; WP_070246368.1; NZ_LROM01000047.1.
DR AlphaFoldDB; A0A1E7X669; -.
DR PATRIC; fig|762836.4.peg.699; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000175989; Unassembled WGS sequence.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 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; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; 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; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 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; 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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
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:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:OFA08529.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000175989};
KW Transferase {ECO:0000313|EMBL:OFA08529.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 290..359
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 425..646
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 683..799
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 883..980
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 843..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 732
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 922
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 983 AA; 106880 MW; A3F8F0B5E294AFC4 CRC64;
MLTSGTSTSR FNAARLLLWG AGWALAVAVG VAAYFVGERI VDADARQRFD HVARSTQYAI
SVRIKAYAGV TRGLAALVRA SDDADRRQIL RYVDGLDLPR QFPAVVSMTW EPDPGAAVVV
HPGTAPAGAE GVLGMRLPVY RPGLAQADAA QRRAAYRGMV GLNFSVARLM QVVLDETMVR
GVQLDLYADG SVDADRRRLV IEPRDRLLFS ERGAEPVAAM ATADYFESVL PVDFNGALWK
ARFRVRKQAL RNGFDVYFPL AAGVAGGAGT LLLYSYLAVL YRSQRRAVKH RVLLDTVLNN
LDAHVYMKDQ YRRYLYVNPK MAEHLGLPAA QIVGRRDREL MPEEKADAAW ALEQPVFADG
LKRASETQHA GHGGVTQYHW SVRVPVTLGR SVAAVIGVST DVTEMHRLKQ RADTANRAKS
DFLSNMSHEI RTPMNSIIGM AHLALKSVTH PKQRDYLQKI YHSGQHLLGI INDILDFSKI
EAGKMDLEVL DFSIDRLLTN LTSQLGDLAT ARGLELVYDI HPDLPRQLRG DPLRLEQVLI
NFTSNAIKFS ERGRVHVRAC LLEQHDQHLL VRFEVQDRGI GMSENQVAQL FQSFQQADNS
TTRRYGGTGL GLAISQQLAE LMGGRVGVES RPGAGSTFWF TARLDLPFDA LAVADDPGAD
GGAGANAADP LQAGLFESLR GASILLVEDN IFSQQVGQEL LEDGGATVCV ANNGKEAIDL
LLKERFDCVL MDVQMPVMDG FEATRLIRAH PKLSGTLVIA MTANAGREDQ QRCMDAGMDE
FVTKPVAPRL LFATLAKWLA QRAAAPSAAP RPLAPPPSFF TMADGSATAA GAAVLQAALA
DLRPDAPHPQ PAQPQALPPS PPAAPAEGDL FDIAALAQTF AGKPDKMRKY TLLFLESARE
TMVEIDAALA AADLARLSEL GHRLKSSARA VGAMRFGNLC LALEQGRRDA DIARACALVA
QMHALLLLLG PQMEQELLAY DPG
//
