ID A9KQ78_LACP7 Unreviewed; 633 AA.
AC A9KQ78;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cphy_3033 {ECO:0000313|EMBL:ABX43390.1};
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX43390.1, ECO:0000313|Proteomes:UP000000370};
RN [1] {ECO:0000313|Proteomes:UP000000370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg
RC {ECO:0000313|Proteomes:UP000000370};
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) 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};
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DR EMBL; CP000885; ABX43390.1; -; Genomic_DNA.
DR AlphaFoldDB; A9KQ78; -.
DR STRING; 357809.Cphy_3033; -.
DR KEGG; cpy:Cphy_3033; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_1_9; -.
DR Proteomes; UP000000370; Chromosome.
DR GO; GO:0016020; C:membrane; 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; 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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABX43390.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000370};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..391
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
SQ SEQUENCE 633 AA; 73964 MW; 7B8E932881FF5CA0 CRC64;
MLKILKINKM KKQNKRKYLG LKGRMLLGIL QVLIPIMIVI TILFWNTRKV MKQEYMRTTQ
SRVTEIANKI DAKLTDIYSV SDNFAANDQL DKYIEKVYSP QEQIYKKLDI VRIYSNIFSA
YDILNKRERI SAIYTYKGEL FNFLDPNKNT KEVIEKLQDM NIEDPDLLMK FRWFPVQDNF
LLSDYPEGIR EQKAVMGIRR IYSWEKGKYQ YVQLFALKEK EIYEQYVQLA ESIPGDIYIL
TGDGSLISSS NEEVVKAGEI SSKLKDMILE RTKDSQEMQD SSGHKLVNVK VSEVNDWMTV
MIIPVNAVTR DMDMLYLRIF LVMMVCVGLC AIMVLYLYKS FMDPIGELNA SMKEVYGGNL
NAYIEVKQKN EMGDMIRYYN SMLEQINTLF IEDLKAERKK KELELEVLMS QINPHFLYNT
LENIVWISND AGRPDIGRMA ASLGRMYRLS ISGGQVIVLM EHEIEHLMAF VNIQKNRYKE
EFEFDLRTDM QQIHGLYSLK ILLQPVVENS FLYGMTGLKH PMLIRVTIKE KDGWVTIKVM
DNGRGMDKEQ LKEIRNQIRF GRTEKAEQER NRRSTGIGLH SVEMRIKLYF GVDHAVSIYS
KKEVGTLTVI RIPKITKDDV DERGNLIENK RIK
//
