ID A8TV86_9PROT Unreviewed; 1188 AA.
AC A8TV86;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BAL199_07218 {ECO:0000313|EMBL:EDP63503.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP63503.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP63503.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP63503.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP63503.1}.
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DR EMBL; ABHC01000013; EDP63503.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TV86; -.
DR STRING; 331869.BAL199_07218; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000003417; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 2.10.70.100; -; 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; 5.
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; IPR013767; PAS_fold.
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; 1.
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; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF12860; PAS_7; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 4.
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; 1.
DR PROSITE; PS50112; PAS; 2.
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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EDP63503.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Transferase {ECO:0000313|EMBL:EDP63503.1}.
FT DOMAIN 20..67
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 201..253
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 388..428
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 678..899
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 922..1039
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1089..1187
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1041..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 630..671
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 971
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1128
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1188 AA; 130082 MW; 574CBF7B58930BC8 CRC64;
MASLIRSDVA GQLGVDVGSL VDAIDDAIIA FDPAGTIVAW NPAAERLFGI VTTDAIGGPR
SLIEPEDDPA GWFDGVLGGR PRRFRGRRTD AQHNPFPVDV TASPIVNADG AVQGVVQTLR
RAPMEDSRPL IELAEDMAWI GHWRIETPGD RHVWSAQTYR IHGIEPGTPM SSANASALYH
PDDRERVAAA VNQAIRFGVD IAFEAKIIWP DGTVRKVACR GTTERGRDGK ATAVVGVLQD
LTDQIAARET LAERNRALAI LRETVEIVPY SISVYDEHDR FVLANRKYFE LYPYLENETK
LIGKTFEDVL RISLQNKVIM DRTALEDPEN YVAARMADRR GGLPMAERRL ANGHWYLIRE
NRTTSGHTIS TRIDITEQKQ AQLELGRTME VLQATLDTMP NALIAFDADN RLMAWNSAFV
SLVGVEPERF ERGRPLRGLT KDVLAKLPST ETGIRPMFLH IARRSPADFE WRRNDGEIYA
VLGRPMPNGG YVTLFRNVTT ERRAQVRAAQ FEHRLSNALE LMSEGFALFD ANDILILCNE
TYRRMYGKST AYIRPGRRFV DIVRDAAATG QFPAAVGREE EWVAERLELH RNPPDQPTLQ
ALADGRVLLV AENRTSDGGS VGIRSDITER VRTENDLRAA RDELEEQAQS LRDLAEQIDA
ARLRAEEAGA AKSRFLAVMS HELRTPMTGL LGMIELASRT ELSKEQQGYV RIMRDSAETL
LALLNDILDF SKLEAGKVQL EEITFAPEQI IGDVFGLFQA QASAKGLVLE ADLRPSVPAW
VRGDPLRVKQ ILSNLISNAI KFTTKGRITV RLGATEGPSG LVRLQGEVID TGQGIAAGVL
EHLFQAFEQG DSSTTRQFGG TGLGLAISRR LAEGMGGSIT VESELGRGSV FRFAVLVRVS
TVPAVEDQRL ADEDELPTLP RRILLAEDND VNRMLVSKVL GQSGHQVDEV ADGQQALQAA
TRVTYDLILM DMQMPVMDGV EATRAIRQLP GAAATVPIVA LTADALPEHR HIYFDAGIDE
LLTKPVDWRL LDRTIARLGG REGASGTATG GEASAPTPPR ETPLESPSVA DDVPVFDVTR
VEEVLGVLPP KRVAGMLSML PSEIELRLAE FQSALDDKDL VRARRAAHTL KGLAANFGAT
QLVSASRAAE VACDTLDGGQ AALSGMAEVA KRTSAAAVEL SATFRARQ
//
