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Database: UniProt
Entry: A0A0Q7T913_9CAUL
LinkDB: A0A0Q7T913_9CAUL
Original site: A0A0Q7T913_9CAUL 
ID   A0A0Q7T913_9CAUL        Unreviewed;       601 AA.
AC   A0A0Q7T913;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASD25_19490 {ECO:0000313|EMBL:KQY91332.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY91332.1, ECO:0000313|Proteomes:UP000051815};
RN   [1] {ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY91332.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY91332.1,
RC   ECO:0000313|Proteomes:UP000051815};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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:KQY91332.1}.
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DR   EMBL; LMFL01000008; KQY91332.1; -; Genomic_DNA.
DR   RefSeq; WP_056615477.1; NZ_LMFL01000008.1.
DR   AlphaFoldDB; A0A0Q7T913; -.
DR   Proteomes; UP000051815; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.250.3020; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR033479; dCache_1.
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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PIRSF; PIRSF036431; STHK_DctB; 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; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          391..601
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          320..382
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   601 AA;  64635 MW;  3AA8F3EAEE04FF6C CRC64;
     MRDPASSTTQ WRLFATAWIL VAILVVWVSG EVARQDARAS AGRQAATASA LHAAVLRSEL
     ERHRSLPMVL AQDPDLAALL GKPDPTSVAR LNRKFEALAT EVRAAAIYAL DANGKTLAAS
     NWKLPTSFVG SNYRFRPYYF EAMRNGQAAF FALGTVSGRP GLYLSRRVDD RTGQPLGVIV
     AKVEFDALEA DWRASGEPTY VTDADGVVLI TTVPAWRFHA ARPLSADLRR RLAATQTAGA
     TVPTPLPFDT RNGALVRVSA DVPADLYAVA SDSIPDIGWE LNLLSPAGDA EARAVAVARW
     LGALTVGLLA ALTGILLRRR QRAAARSIEA EQARVELERQ IDLRTSELRS TNDLLNHEIE
     ERRRLESVRQ DLQDDLIQAN KLATLGQIAA GVAHEINQPV AAIRTHADSA SVQLRREDNA
     GALRSLANID RLTERVGAIT DELRAFSRKT RSETVAVGVD AAIDGALLLV AGRMGEKGIV
     LNRRRAPSGL AVRAERNRLE QVVLNLLQNA IEALDGVANP TIDVGVVVKG KQAVIHVSDN
     GPGVAAGVQE RLFTPFTTDK QDGLGLGLVI SRDIVAGFGG ELALEPSTRG ARFIIRLAKA
     S
//
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