ID A0A2U2HES5_9BURK Unreviewed; 1471 AA.
AC A0A2U2HES5;
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=C7C56_023140 {ECO:0000313|EMBL:PWF42252.1};
OS Massilia glaciei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF42252.1, ECO:0000313|Proteomes:UP000241421};
RN [1] {ECO:0000313|EMBL:PWF42252.1, ECO:0000313|Proteomes:UP000241421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B448-2 {ECO:0000313|EMBL:PWF42252.1,
RC ECO:0000313|Proteomes:UP000241421};
RA Wang H.;
RT "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang, China.";
RL Submitted (APR-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:PWF42252.1}.
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DR EMBL; PXWF02000300; PWF42252.1; -; Genomic_DNA.
DR OrthoDB; 9813903at2; -.
DR Proteomes; UP000241421; 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; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.20.20.450; EAL 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 InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003660; HAMP_dom.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 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; SSF141868; EAL 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; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000241421};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 202..254
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..495
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 512..628
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 649..767
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 801..894
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 911..1027
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1070..1205
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 1211..1465
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT MOD_RES 566
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 698
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 840
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 960
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1471 AA; 159896 MW; 9F9AA4DF12D4C126 CRC64;
MLRYFLRHVG FRRQLTIIVS AAIMVLALFS SLMNSWEASA RMRGHFVEQG QRIAENMARQ
STLALLYHSG ENARDAVATT LTFPDVLGVR IVDLKGRVVL DQRRRQLAAS GAPAVPQPAA
AAAAPLRETE TAWHFSAPVY NGATEASPFD PQEQKPVLLG HVQVEMGKGT LTRLSLSLLI
GNLIITFSFA VVLLIVVGML TRHMINPLNA LSRLMRRAES GESGMRAAPA GPRDLIEMAL
AFNQMMNVLE QRETELKGAR DAALNLALMK AQFAATVSHE VRTPLNGVVG MLDMLREMNL
NKRQAECVEV AWSSSRTLIE LINNILDFSK MEAGKLTLDE TDFDLRTLVE EVIELVASQA
QQRDLELGYL IGPGVPERVH GDPLRLRQVL INLLSNSVKF TEHGEVSVFV SRSGGERFGL
RFEVRDTGIG MSGEDQGRLF ESYAQADPST SRKYGGTGLG LAIVKQLVGL LGGEIGVVST
YGEGTTFTFN IACQAAQPLP ADPADATLAG LRVIAVDDSH IVRSFLEQAL GRHGVDCHST
RWGGAALEQL KAGADAGKPY LIVIMDIGAV DDGGNDLAHQ VGIEAPGTLV LMLDRLGAPS
GGTLADGFPV LAKPLREERL LRALREMVGG APAPGRALQV GAQTRRQYRV LVVEDNRTNQ
MVAAGMLTMS GCECEFASNG REALEATRHR QFDLILMDCC MPEMDGYEAT AHLRAREAGG
GRRTPVIAMT ANTQPGDAAR CLEAGMDDYL PKPITLAELR NKLDSWLPGA DQAHTLHGHE
RGGDDDNPLD LAVLVKLREI LGASLPQAVS PFLEDTPQYL LELEAAVHGG DLENARAKAH
VIKGSAGNLG ATRLAQLAKE AEEHATAGAL ALAAPLLPRL RVAYNAVAAA LASAVVGSDG
GGQAAGDGVP QVLIVDDDRS TRSTLRHTLQ RDGFRVEEAA DGAQALAMLK RFHPDVILMD
AVMPVMDGFT ACARMQELPG GRAVPVLMIT ALEDNSSVER AFAAGASDYI PKPIHYAVLS
QRVRRIIEAN RAEKRIRHLA YNDLLTGLPN RTLFFDMLGE AVQEASRSKA MLAVLFMDLD
RFKYVNDNLG HDVGDRLLVA VAQRVRRVVR SIDVVARLGG DEFTVVLSEV EGAAPAAAAA
QNICRVLAAP FQIDGHDIFV TSSVGIAMYP HDGSDVATLV KHADTAMYRA KKTNTGFQFY
EASMEQSISE HVRMESDLRR ALENGELEVF YQPQARFDTE QIIGMEALVR WHHPTRGDVV
PVEFIPLAEE TGLINRLGEW VLRTACAQAQ QWRVEGLPMM RLAVNVSVRQ LLQKNFAATV
EAALVDTGLA PELLELEITE STLMEHAQDT LQALDRLRQL GVRLSIDDFG TGYSSLSYLK
RFPVDIIKID RSFVRDVPQD ADDAAIVTGI IALAHSLRLE VVAEGVETEA QRAFLRGQNC
DLLQGFWLSP ALPAEGFSEL IREREAKLLR A
//
