ID A0A1S8TXK1_9CLOT Unreviewed; 602 AA.
AC A0A1S8TXK1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=ypdA_1 {ECO:0000313|EMBL:OOM82461.1};
GN ORFNames=CLPUN_01630 {ECO:0000313|EMBL:OOM82461.1};
OS Clostridium puniceum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM82461.1, ECO:0000313|Proteomes:UP000190890};
RN [1] {ECO:0000313|EMBL:OOM82461.1, ECO:0000313|Proteomes:UP000190890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM82461.1,
RC ECO:0000313|Proteomes:UP000190890};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) 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:OOM82461.1}.
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DR EMBL; LZZM01000011; OOM82461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8TXK1; -.
DR STRING; 29367.CLPUN_01630; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000190890; 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; cd18773; PDC1_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 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:OOM82461.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000190890};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOM82461.1};
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..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..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 422..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 602 AA; 69693 MW; 92B7CD13006E3CD1 CRC64;
MKHNNWRIKN LINNVKIRNK LILTYLIVTI ATVSIVGTYL TTQMTTIVVN RAVDEAENNS
KTIQHRLEEI LNLTTKVSDM IYGDENLNSI LTRNYTSYNE VIETYYNYSV LKNYLKYYRE
FSSITVYVEN PTLLPNTEFL MVSDTIRNED WYKKAIANSG KIAWRYTKDE FTNLEYLSLV
RCIKDNRGKQ TGVLVISINP SILKGLIDTD PSNNMILLDG QTISSKNKYE IDEKQLTKYI
IKKSQKDDIN VFKTEFNKQE SYMILNSFKI DKTLENNFKI LIIVPINQIT NQTNKVTTNS
IVVILITIIF ALFIIIYFSK TISERVDILR REMHRVVNGD FYIVSRIEGS DEIGQLYQDL
KTMIKSIKQL IEEVYIEKIQ KEQLRASQKE AEFKMLANQI NPHFLYNTLE TIRMKAFCNG
DKEIADIVKK LGKIMRRNLE VSGKSVSLKS ELDLIESYLQ IQAMRFEGMV KYELNIESSV
NQDEYEILPL LLQPVVENAF VHGLEEKREK GTIIIDILEK DECLIIKIND NGVGLEPKKL
EKINKKLVLS EENNGKSIGM INVNQRIKIR YGKQYGLNIE SEFGKGTTVT LSLPIIDKTE
VL
//
