ID A0A0Q4C277_9SPHN Unreviewed; 469 AA.
AC A0A0Q4C277;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE49_07670 {ECO:0000313|EMBL:KQM18986.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM18986.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM18986.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18986.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM18986.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM18986.1,
RC ECO:0000313|Proteomes:UP000050893};
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 -!- 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:KQM18986.1}.
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DR EMBL; LMJY01000016; KQM18986.1; -; Genomic_DNA.
DR RefSeq; WP_056771975.1; NZ_LMJY01000016.1.
DR AlphaFoldDB; A0A0Q4C277; -.
DR STRING; 1735670.ASE49_07670; -.
DR OrthoDB; 913606at2; -.
DR Proteomes; UP000050893; Unassembled WGS sequence.
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 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 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQM18986.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050893};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..247
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 255..464
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 469 AA; 50196 MW; 6550DB8E76F5AD5D CRC64;
MPAEPGGGPH RAIALRTRLL AAMLGPLLAV AAIIGIGGAA LIADVVRRTN DRVLGGALGA
IAETVEVERG EVTLDLPPAA FGMLENSERD NVYYRIAAGN QLLTGYADLP APDPATLTTD
EPRFRFARYR GQDIRIGEVK RMLPRIDSPV IVQIAETLDN RKALTRRLLD ALLIAELALV
GVATLLLRPA LSWSLRPLAR LRGAVESREL SSRPDFSPLD SGPLPRELRP LATAFNQLLA
QLDHATGGVR RFTADASHQM RTPLSVLKVQ VALARRGSRE ALDEIGDAVT RLERLVTQLL
ALARAEEAGV SAPLESVDLR EVSAAIIGRL INQAIGAGVE LNLDADDGED YVISGHRTLT
FEIIANLVDN GIRYNRPGGT VTITLLQRAS ETVLTVGDDG PGIPPDKRET IFERFVRLEA
AQGPDGTGLG LAIVRSAASR MGASVEIGEG AIGTAILVRF PKRSLESRQ
//
