ID A0A255HW79_9BURK Unreviewed; 1139 AA.
AC A0A255HW79;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CD932_07540 {ECO:0000313|EMBL:OYO30993.1};
OS Janthinobacterium sp. PC23-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2012679 {ECO:0000313|EMBL:OYO30993.1, ECO:0000313|Proteomes:UP000216749};
RN [1] {ECO:0000313|EMBL:OYO30993.1, ECO:0000313|Proteomes:UP000216749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC23-8 {ECO:0000313|EMBL:OYO30993.1,
RC ECO:0000313|Proteomes:UP000216749};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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:OYO30993.1}.
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DR EMBL; NJGY01000001; OYO30993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255HW79; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000216749; 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; 4.
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; 4.
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; 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; PF13426; PAS_9; 3.
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; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:OYO30993.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:OYO30993.1}.
FT DOMAIN 165..218
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 213..267
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 334..398
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 408..460
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 534..586
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 622..843
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 879..995
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1036..1132
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 928
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1075
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1139 AA; 124843 MW; 7933DCF650081E10 CRC64;
MHLSHRSLTR SSARRLRRLA PHPLVLLLAC GWTALARAAP ALGEGAAGPW PWLAASATAL
AGIATWQAWR WRRQLQGVQS GEISDKGIGT PAAQALQGAV LAGWCWQRGG DRLSMSSLYR
SLLGDKKASL QLTLADWLAE VHRDDRARLS NALRQHFDGQ APAPVSCEFR LRHGDGQWRW
LLLRGAVLVR ASDGAPVKAS GVLCDIAERK ADEQARMRSM LEAAPEAMLI ADIEGRVHFA
NQIGARCFGY PLADIIGISL EQLVPDSTQG QTAGEAQSRH SLPGRVMMAR RRDGSHFPAK
VSLSQLRMAG QVYSIVSLRD MTQRQRAEEA LHASSERYRL IVQTAAEGIW MTNSAGLTTF
VNPKMAHLLG YTVQEMLGRP LLEFMDRDSQ LLMQRRLDSH GNLHSQPDQV DFRFFRKDQS
SMWGLLSSSS IQSDNGEPGG TLAMITDITE RRQASIALSN SSQRMASVFG AVTNGLVVQN
SDGHILESNA AAERMLAASR AGGSLWQAIR EDGSPFEQHS HPVHITLSTG EAMRDVVMGV
QQLDGNLCWL SVNTEAIRDE YGKVGMVVAS LTDITYHKRS ESTLRELNEH LEERVAQRTE
QLDQAKQVAE EASLAKGQFL ANMSHEIRTP MNGVIGMAYL ALKTDLEPRQ RDYLEKIRFA
GEHLLGIIDD ILDISKIEAG KLKIEHVNFS FDHVIQTLNT VVAPRAAGKN LELLFEIDPQ
LPPILVGDPL RLGQVLINYA NNAIKFSDQG SITVIVKKVV GDDKHCLVRF EVCDHGIGLS
HDEMSKLFQS FQQADTSTTR EYGGTGLGLA ISKQLAQLMG GEVGVDSCPG LGSTFWFTAR
LGISSQAAPA LLDTMLETAQ AMRASADAAL VMGALKHARI LLVEDNTFNQ QVALELLEEA
GASVCLANNG VEALDLLRQA QFDCVLMDVQ MPLMDGLQAT RLIRADPRLA QLRVLAMTAT
ATSEDRVRCL EAGMDDFISK PIQPAMMYQT IAGWLPAREA PPPPVRSRNA PAFKTTLAGD
PQVIDLSILA KLLGYNPQKV RKFAFKFLQT TQDGFADIDA ALARGDVAQV RELGHRIKSS
ARTVGALGMS ELCHQLENLP PGTNADEIEQ AHRIVRLLWP LLEQITEQIM NNTSFANDD
//
