ID F4QUB1_9CAUL Unreviewed; 1042 AA.
AC F4QUB1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABI_47590 {ECO:0000313|EMBL:EGF89411.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF89411.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL883081; EGF89411.1; -; Genomic_DNA.
DR AlphaFoldDB; F4QUB1; -.
DR STRING; 715226.ABI_47590; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_44_5; -.
DR Proteomes; UP000006512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00130; PAS; 3.
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; 3.30.450.20; PAS domain; 3.
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; 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; 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; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
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; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 293..364
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 415..485
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 489..541
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 535..605
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 679..896
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 916..1029
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 965
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1042 AA; 112801 MW; F72F8D8B14053B60 CRC64;
MEAAIDWLRL SRRLGVAVCA IGLIALVGWP TDIVLLRSVL PGLMAMQPTT AMCLVLIGSV
LALPGLPRAL SLSACAVAAL WSLAFLVEHL TGATSALDTL LFGDKILHQA PLPAHPGRMT
EGTSLGLFLL SSLLLIHRVI GARLPAALHL LIATVPLAIG AISLLAYLLA VRSARGVVGY
TDIDLHTSVG LCLLSCAVMA LRPDATPLRV LAQAGSTGQL MRRILLTVVA LPPVLGWTAL
QATNLNLLTP DFRLVLTTAG TMLGLIILGV VSARRMSESE NRLESERLRA QASEAQFHSV
IANAHQAIVT TDEHGRVASW NGQAEAVFGW SETEVVGRRM SDMIIPERFR DAHTKGMARF
METGEARVIG QRIELPALNR SGTEFTIELA LSAARNSAGW QFTAMMHDVT ERLAQTQLFE
AAFHHAPIGV ALVGLDGGFL KVNLAFCRLV DLEREDLLAA DFQKITHPDD LDRDLELLAE
LTRGDIPSYQ MDKRYLRPNG EVVWVNLSVS MVREETGAPK HYIAQVQNLT ERMEAEARYQ
LMAENTTDLI VTCDLNLRRS FVSAAVRRLQ GISPAEALAC RPEDYMHEED VASVVATFRR
TAEGETGLRV RWRCWNQEAH IWTWVESSPS LIRNGDDTAP MFVDVVRDIS SQVTQEQKLE
AATDAAEAAA AAKADFMANM SHEIRTPLTV MIGFSSLLTE RQDMPDDALR YAQRIATASN
SLLSLVNDIL DFSKLEAGQL ELKPKPTEIV EMSRELFLMM QAQAAAKGLN LRFEDDNSVP
DTVFLDPQAY RQVLLNLVGN AIKFTDTGSV TLMLGYDNKH LTVRVIDTGP GMNEAGQAKL
FQRFSQVDGS STRKHGGTGL GLAICRGLVE AMGGTIGVTS APGEGSHFHF TLPAPALADG
AAFEFDTDLP DLAGLRVLVV DDNSVNRELA RAILERADAA VIEAEDGSAG VLMAGVYPLD
VILMDIRMPG MDGTMAAKRI RSEPGPNRDV PILAFTANGH DLYNPADFDG LVAKPITPAA
LVNAIARAAG SESADMDQSL RA
//
