ID A0A3D9IAI8_9BACL Unreviewed; 646 AA.
AC A0A3D9IAI8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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=DFP95_10875 {ECO:0000313|EMBL:RED58549.1};
OS Cohnella lupini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED58549.1, ECO:0000313|Proteomes:UP000256869};
RN [1] {ECO:0000313|EMBL:RED58549.1, ECO:0000313|Proteomes:UP000256869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8236 {ECO:0000313|EMBL:RED58549.1,
RC ECO:0000313|Proteomes:UP000256869};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RED58549.1}.
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; QRDY01000008; RED58549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9IAI8; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000256869; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RED58549.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000256869};
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 40..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 359..411
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 521..638
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 646 AA; 73060 MW; A053233BD9CF5C47 CRC64;
MQARESRSCY NGGNNFIIRA REGFGVRLGK IYRNYIHNNL FIKVIFVFAI IVNLTIITLS
YLLFNLMSAS IVSSELNNQK QAMDRVNRYM EQKYDWVQNA VQDIYRNGLL ASNASYFLRH
PYQDYVQYML DQNFAGGNES AADILSYLSN RMESDPDIQN VLLYSSEMQQ LYVFNSNGPR
KLYSTNPIRS YIPEIMAAEG PVAATPNTWI RRLIGQWNPQ LYSMRSQVND KNTLKNIGQL
LVYFDAGMVN RSLEQNRAPL KGAILVLTSD GQVLADTSNR YYGMTFPYME QLGSLKEVVT
LDEPSYISTL TQNKAGYIVV GISPKSIIAE AYAGLKRTII LISSACIAVA VIIPSLVIFN
IARRTNRIVH FMRKVEGGDL KARLQDSRED ELGQISHSFN DMLDELDRHI DREYKAEIRL
KQTELAALQA RVNPHFLYNT LEVIRMRAVS QGAADVGDMI YSLAALFRNS VSVRPVNTLG
EELEMCRLYL ELFRIRYKNK FTYTIECESE ITNIPVFKML LQPIVENYIV HGMESRRKDN
RLAIDAAMKD GIVTVRIRDN GKGIEPDLLE RLTQALDLPE PESEHGQAQG QGSGSGQSFG
LRSVHDRIRL VHGPAFGISI ESEPGSGTLV AVSWPIVTEG EKTEDV
//
