ID A0A1G8CB92_9BURK Unreviewed; 936 AA.
AC A0A1G8CB92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216320_11351 {ECO:0000313|EMBL:SDH42619.1};
OS Duganella sp. OV458.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855290 {ECO:0000313|EMBL:SDH42619.1, ECO:0000313|Proteomes:UP000199454};
RN [1] {ECO:0000313|EMBL:SDH42619.1, ECO:0000313|Proteomes:UP000199454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV458 {ECO:0000313|EMBL:SDH42619.1,
RC ECO:0000313|Proteomes:UP000199454};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCD01000013; SDH42619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8CB92; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000199454; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00156; REC; 1.
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; 6.10.340.10; -; 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; IPR033417; CHASE8.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF17152; CHASE8; 1.
DR Pfam; PF00672; HAMP; 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; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
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; SSF158472; HAMP 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDH42619.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..245
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 285..506
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 522..640
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 682..802
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 838..931
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 575
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 731
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 877
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 936 AA; 100805 MW; E449AC4F4971AED1 CRC64;
MFQFERSGLS QKLSIMSVLS IGSALLLVLA GFAATSVLSH AEVARQQLSS LAGVIGSNSR
TALMYADRQQ AELTLATLAV EEDILQAALY GSDGKLLARY LSPRLPAAQT GPAELDALAG
AAEIHAEHSG PPWAPALRVY RVLRDGEDVA GVVMVEASQM RIWLDILKNL GAAVVAAALA
FMMALLTAAR FKGGFAEPVS KLIAAAQQVS RGHATPRILH QRHDELGALI DSFNDMLAQV
EGRDAALAQY RDQLERQVSV RTEQLEKAKN AAEAASQAKS AFLATMSHEI RTPMNGVLGM
TELLLATRLS EQQRHYTSMV KRSGEHLLVI INDILDFSKI EAGKLTVEYI HFNFRDLLDD
IDNVFSPQAE AKGLRLELDV DQRTPLGVFG DPNRLRQVIF NLLGNAIKFT DGGQITVKVM
VAREDAQSVA LRFEVRDTGI GVSAEARARI FDSFSQADGS TTRKHGGTGL GLAISKQLVE
LMGGTIGVEH ALTQGSIFWF AVNFDKRRVD IDDPSTATQG IRALIVDEHP ASRAALEQHL
AAWRVTCAHS SASDALPRLT QAAAQGRAYD VVLLDMEQPR TSGLALAAAI RAEQPGLRVV
LLSTERDAAD DVQRREAGVA FQLIKPPRDG DLYDAIAAPA RSRDVRGAAE PTLLPSAAFA
PAALPHGTLS TGSATRQRRR RKVLLAEDNP VNVEVASAML EGLGLEVSRA CNGEEALHSV
QADDFDLVLM DCQMPVMDGF AATSEIRRHE LQHGRARSLP IIAITANALQ GDRESCLAAG
MDDYLSKPFT QQALGQTLSR WISLPRTAPM PNEAPSTDDD IIQQQALDNI RALSPANGDA
LLERVLQAFL HDTPAQLQAI RQAIASDNAG QMRKAAHSLK SSSANVGAQA LAQRCKDVEQ
LGRNNTTAGA AALLAEMERS FQAARQALGA MLEKEF
//
