ID U9ZYE3_ECOLX Unreviewed; 559 AA.
AC U9ZYE3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1620_03631 {ECO:0000313|EMBL:ESA89912.1};
OS Escherichia coli 909945-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1269007 {ECO:0000313|EMBL:ESA89912.1, ECO:0000313|Proteomes:UP000017275};
RN [1] {ECO:0000313|EMBL:ESA89912.1, ECO:0000313|Proteomes:UP000017275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=909945-2 {ECO:0000313|EMBL:ESA89912.1,
RC ECO:0000313|Proteomes:UP000017275};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUN-2013) 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:ESA89912.1}.
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DR EMBL; AXUK01000181; ESA89912.1; -; Genomic_DNA.
DR AlphaFoldDB; U9ZYE3; -.
DR PATRIC; fig|1269007.3.peg.3336; -.
DR HOGENOM; CLU_020473_3_3_6; -.
DR Proteomes; UP000017275; 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 GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR CDD; cd16955; HATPase_YpdA-like; 1.
DR Gene3D; 1.10.1760.20; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR InterPro; IPR047965; YpdA-like_HATPase.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:ESA89912.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..548
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 559 AA; 61886 MW; 6E7FF069152B58EA CRC64;
MLLAVFDRAA LMLICLFFLI RIRLFRELLH KSAHSPKELL AVTAIFSLFA LFSTWSGVPV
EGSLVNVRII AVMSGGILFG PWVGIITGVI AGIHRYLIDI GGVTAIPCFI TSILAGCISG
WINLKIPKAQ RWRVGILGGM LCETLTMILV IVWAPTTALG IDIVSKIGIP MILGSVCIGF
IVLLVQSVEG EKEASAARQA KLALDIANKT LPLFRHVNSE SLRKVCEIIR DDIHADAVAI
TNTDHVLAYV GVGEHNYQNG DDFISPTTRQ AMNYGKIIIK NNDEAHRTPE IHSMLVIPLW
EKGVVTGTLK IYYCHAHQIT SSLQEMAVGL SQIISTQLEV SRAEQLREMA NKAELRALQS
KINPHFLFNA LNAISSSIRL NPDTARQLIF NLSRYLRYNI ELKDDEQIDI KKELYQIKDY
IAIEQARFGD KLTVIYDIDE EVNCCIPSLL IQPLVENAIV HGIQPCKGKG VVTISVAECG
NRVRIAVRDT GHGIDPKVIE RVEANEMPGN KIGLLNVHHR VKLLYGEGLH IRRLEPGTEI
AFYIPNQRTP VASQATLLL
//
