ID B9Y5E3_9FIRM Unreviewed; 499 AA.
AC B9Y5E3;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HOLDEFILI_01025 {ECO:0000313|EMBL:EEF68818.1};
OS Holdemania filiformis DSM 12042.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemania.
OX NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF68818.1, ECO:0000313|Proteomes:UP000005950};
RN [1] {ECO:0000313|EMBL:EEF68818.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68818.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF68818.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68818.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL Submitted (FEB-2009) 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 -!- 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:EEF68818.1}.
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DR EMBL; ACCF01000057; EEF68818.1; -; Genomic_DNA.
DR RefSeq; WP_006058234.1; NZ_GG657553.1.
DR AlphaFoldDB; B9Y5E3; -.
DR STRING; 545696.HOLDEFILI_01025; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000005950; Unassembled WGS sequence.
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 CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF68818.1};
KW Membrane {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 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 189..241
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 256..469
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 472..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..260
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 480..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55472 MW; A861B10C387B59E5 CRC64;
MKLRHQLALS AFAVFALIFS GSGLTLIEIS ARLRQQDQID ALIAQNRAID GMLSSAAALM
AFTPSSFSPQ RQLQNQLEKI LADSALETGV RILDEEGRIM ADSGFPEIDD DQMETPQNDQ
IWMKIKNTAA GPVLISAHVL PLNDTRLIIQ SSADLGALRR NVQNQLGLFF FINLAAYAVY
WLALIVVSRR LTQPVEQLAE GERQIAGGRW SQRVPVSGAQ ELKTLAENFN RMAETVEQKV
AELETENQEK EIFINNLSHE MKTPLTSILG YTQLLRRTKM SPQDAEQALD IIESEARRME
RLSSRLMQLI VAARPLSECS AAALDSFIEQ AVLRLKPALR EKSLRLCVEC EPLTVLIDEE
LMQAALRNVL DNAVKASQPQ TLITIEAKTT ETGWQITVRD EGCGIQDPHP ERMLQPFVME
DQARSRKHHG AGLGLALTQR IVQAHGGMVE IDSQPGHGTE VRFVFPPETL AADAKAEASQ
TKARMGKSEQ DKEKTHEEQ
//
