ID H1LY30_9FIRM Unreviewed; 595 AA.
AC H1LY30;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9099_02391 {ECO:0000313|EMBL:EHO50623.1};
OS Lachnospiraceae bacterium oral taxon 082 str. F0431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO50623.1, ECO:0000313|Proteomes:UP000003005};
RN [1] {ECO:0000313|EMBL:EHO50623.1, ECO:0000313|Proteomes:UP000003005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0431 {ECO:0000313|EMBL:EHO50623.1,
RC ECO:0000313|Proteomes:UP000003005};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHO50623.1}.
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DR EMBL; AGRL01000143; EHO50623.1; -; Genomic_DNA.
DR AlphaFoldDB; H1LY30; -.
DR PATRIC; fig|861454.3.peg.2231; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_1_9; -.
DR Proteomes; UP000003005; 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; cd06225; HAMP; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 6.10.340.10; -; 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; 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; PF02743; dCache_1; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHO50623.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..372
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 475..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 595 AA; 67487 MW; C69D3CE8B21BFC9D CRC64;
MDKRQIIKKF SNKNLSIRSS IFIYFTVTAI IAIALISLIM FQRFTDSLNK TIIEENAGII
GQVGESIDSY LRNVMKISDS IYYNVIKNTD ISDDDIKNGM NLLYVNNDNM IEDIALIAGD
GTLIESMPAL RLKDGINVSE RDFFKKSMAE SEYIYFSMPH IRNLFDQNEN SYSWVMSMSR
AVEVTSEGKA TQAVLLINLN YMFFEELFSN VNLGNGGYIY LINDKGDIIW HPRQNEIYAG
RFTENNKYAA GLKDGISIEN IGGKKLTVNV RTIGYTGWKL VGVTGSAAIN VDSMKFRLFV
LFVADLFLFL LAMVNAYISN RISNPISRLD NSVREIESGN LNVEILPSGS YEVQHLGNSI
RNMLSRIKVL MSDLVAEHNA KRKSEFDTLQ SQINPHFLYN TLDIIVWMIE NEKPDKAVSI
VTALAKFFRI SLSKGKNIIT VRDEVEHVRN YLMIQSMRFK NRFEYSIKVD DNVSDYSSLK
LMLQPLVENA IYHGMEFMDG DGEIDVRVFK ENDELYFTIT DNGLGMSEDV VATLLSKDIV
PSKRGSGIGV KNVNERIKLY FGAEYGLFVE SEPDEGTKIT IHLPAIVYGE KNEDK
//
