ID A0A142EMN2_9BACT Unreviewed; 702 AA.
AC A0A142EMN2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AO498_08170 {ECO:0000313|EMBL:AMQ56387.1};
OS Algoriphagus sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ56387.1, ECO:0000313|Proteomes:UP000073816};
RN [1] {ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA Shintani M.;
RT "Complete sequence of Algoriphagus sp. M8-2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMQ56387.1, ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|EMBL:AMQ56387.1,
RC ECO:0000313|Proteomes:UP000073816};
RX PubMed=27174266;
RA Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA Shintani M.;
RT "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT Brackish Lake.";
RL Genome Announc. 4:0-0(2016).
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};
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DR EMBL; CP012836; AMQ56387.1; -; Genomic_DNA.
DR RefSeq; WP_067545835.1; NZ_CP012836.1.
DR AlphaFoldDB; A0A142EMN2; -.
DR STRING; 1727163.AO498_08170; -.
DR KEGG; alm:AO498_08170; -.
DR PATRIC; fig|1727163.4.peg.1695; -.
DR OrthoDB; 9806995at2; -.
DR Proteomes; UP000073816; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000073816};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 447..696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 375..438
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 702 AA; 80425 MW; A80858119D25B8B2 CRC64;
MIILIYSLFT FLFPDFSEII LENEHQIKSY EYLIQEDEVS DISEIIGSKD FTLLENQNIN
FGINKDVVWL RYSLTNNTTN KEKYLFINNP SLDNLNLYVV QNGYVIQEFS GGRLEEFSNK
VIPSKNIIFR INLPLNEQVY VYLKVSSINK TIITASVNDL PVIETLINRE NIVFGVFTGI
IVGLFFYNLF LFFSVRDKIY LIYVIHTLFV WFAQSSILGY TNELLWPESI WLKLKAGVIF
SSLVSIAGIW FLQVFLSTKS FVPKLDKGFL FIYGVYSFIL VNAFFLSITL SYQVLLVTQS
IVVLYVLVVA FSVLKLGYSP ARYYLLAWSI FMIGIFLFVM SEMGIIPTNN FTAYIMPFGS
ALEVVLLSFA LADKINILKR EKEEEQLEKL RVLRENEDLI REQNVLLEEK VRMRTDELEQ
ALKNLQSTQS QLVNQEKMAS LGQLTAGIAH EINNPINFVS SNIMPLKRDI KDIMEVIEFY
RESGEKQFSP ELKKEAKKLE EDLELDYVLE EVDQLLKGME EGAKRTVEIV KGLRLFSRVD
EQDVKKVDLH DGINSTIILL NSSIPGKIRI LREFGELPMV ECYAGKINQV FMNIINNAVH
ALADHLDQIP DPKITIRTHS HPDHVVIEIE DNGPGMPAHI KQRIFEPFFT TKPVGKGTGL
GLSIVYSIIE NHKGTLEVET EEGRGTTFII SLPLHQNAPK YD
//
