ID A0A1S6EV46_9CAUL Unreviewed; 1010 AA.
AC A0A1S6EV46;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BZG35_09780 {ECO:0000313|EMBL:AQR61907.1};
OS Brevundimonas sp. LM2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1938605 {ECO:0000313|EMBL:AQR61907.1, ECO:0000313|Proteomes:UP000189107};
RN [1] {ECO:0000313|EMBL:AQR61907.1, ECO:0000313|Proteomes:UP000189107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM2 {ECO:0000313|EMBL:AQR61907.1,
RC ECO:0000313|Proteomes:UP000189107};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-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}.
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DR EMBL; CP019508; AQR61907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6EV46; -.
DR STRING; 1938605.BZG35_09780; -.
DR KEGG; brl:BZG35_09780; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000189107; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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; 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:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, 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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..531
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..805
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 905..1001
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 812..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 735
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 944
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1010 AA; 107316 MW; B3AB0B98FB372B26 CRC64;
MNRSNFLRFF RLASIDFAFA TAFVLIAALV GWLWFRTIAT SGEAFDHEAE VLAAQGEAAS
SVVLVRVKDL VAFSEAGAED RVAEKLKTAS RTSPYLTDLG YFETRSTVGR SFMAGRGAIG
PAASDREQIA RDLLRSPGLI AVFPASRYPL LFPSADPLDL VFAQTGPAAQ ADQAVRIYYG
RLSLALLARE LSAETHSAAL SSITAESDGM PIAWRANSRP TWSDRLVPAR DRQIAVRFAR
DYSPVFAFSH TSKQTGPLIM VTAGLLAVFL LLAMVVLRSQ RRRVEQAARL RNAVDQAERA
NEAKSTFLAN MSHEIRTPLN GVLGMAELMS RTDLTEQQAL YTGQIAASGS SLLAILNDIL
DVSKLEDGMM AVDPVETDIP QLLQDIGTFY NGQAGQRGNT LMLDLDGSVP RFGLVDPTRL
RQVIGNLVSN AIKFTENGEV TIGARCESDA SGSATLRIAV TDTGLGIGPE EQKRLFERFV
QANDSITRTH GGTGLGLSIC QQLCGLMGGG VSCESELGRG STFVATVRIA RCDRGAPAVV
QQGTVGLVGA SATVRRIAGS ALERAAFAVV HYASFDALAE ALQSGVAPPL AGIVIDEAND
IHEAREGWLS VRAALTGEGS AWSILLADRQ THRSYPSFDR VLIKPFLPEA LGQAAMDLSA
ARPVSALPVA VPPAPVASAP MFTGRRLLLV DDNDVNLIVA SELLQDLGFE VATARDGRKA
IAAADGGNFD VILMDCRMPV MDGYEATRTL KSLMGAGRLR DVPIIALTAN AMKGDRETCL
AAGMDDFLAK PISKRDLVAV LNKLPGLAPK PGLAIDAIPS PPEPMERQRQ PVERPGQIAP
ARAAALKVRT VPSGPEGVRP SPAAGNEGGP VSTVAAALAA SAASAATRQP IALFDPEAFD
ETRRTVRAFG TLIAIYRTDT AGHLEALQRA LSMGNIADGI LPAHTIKSGS RIVGATGLAA
LAEAMETRLR TGRRIEASEL EDLRSRMGQA FAATLVQIDR RMEVSLALAS
//
