ID Q2L1Q3_BORA1 Unreviewed; 812 AA.
AC Q2L1Q3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BAV0100 {ECO:0000313|EMBL:CAJ47706.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ47706.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ47706.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ47706.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47706.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2L1Q3; -.
DR STRING; 360910.BAV0100; -.
DR KEGG; bav:BAV0100; -.
DR eggNOG; COG1840; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_37_4; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013727; 2CSK_N.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF08521; 2CSK_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..225
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 233..444
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAJ47706.1"
SQ SEQUENCE 812 AA; 87745 MW; 121C2EE11A1647DB CRC64;
VFILAVVSLA CASIALFFFL RAYAHRAAEQ AFDRLLAASA LTIAGSVQID DGGVTVEPPY
SSLAMLPPQE RVFYQVLNSA GRVITGYRDL ALSQPLADSA VPRFVYERYH DEPIRVASVG
RLVSASQHAG WVTVRVAETL GSRQALAAEI LNRSLWPLIV VVGVALALLW FGIQRAFAPL
AVVERELRNR EPDDLAPLRA PVPREVRRLS EALNAFMQRL STMMDSLNTL VADAAHQVRT
PLASLRAQAE VALEEPSPER LRERVARIHQ NATQASQLIN QLLMDATIAH RLGRGERLAV
GVAETVNETR RRIGPLDAQR LSISIVPELR RARVMGDRVA LREMLRNLVD NALRHAPDSL
VEIQVTPVAG YRVALTVLDR GPGIAAGDKE RVQQRFERGS SPQSGSGLGL AIVRAVAQAH
GGALALLDRP GGGLLARIVL PLARPAGRGR LAVLLLAGAS LFPALWPSPA PAARLIQESR
YPAPRPSGRV LTVAGPTDTP VFAPLVAGFQ QQRPDVTVVY REMGSLELYE AAVAGQLKDV
DVLISSAPDL QVRLANDGYA LSYASPYLSQ LPTWAVWRNE VFGFTFEPAV IVYNPRRFTQ
ESAPHSRQAL LRLLEREGAS LRGRVATYDI VASNVGYMLA EQDELVSSNF WGLANALGQV
GVRLSPSTNA MLDAIANDEL DLGYNLLGSY ALARQAAGDQ IGVILPRDYM LVLSRSALIA
RSAPNPDLGR ALVDWLLSPA GQQVAASHAG LGALIPGTPG PWSADSLQAL ARGIVQPIVL
SPALLVGLDQ QRQSRFVQNW MRLVTDTPAV PK
//
