ID A0A0A2MCJ5_9FLAO Unreviewed; 804 AA.
AC A0A0A2MCJ5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Q765_13165 {ECO:0000313|EMBL:KGO86005.1};
OS Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO86005.1, ECO:0000313|Proteomes:UP000030152};
RN [1] {ECO:0000313|EMBL:KGO86005.1, ECO:0000313|Proteomes:UP000030152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO86005.1,
RC ECO:0000313|Proteomes:UP000030152};
RA Zeng Z., Chen C.;
RL Submitted (SEP-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 -!- 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:KGO86005.1}.
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DR EMBL; JRLX01000014; KGO86005.1; -; Genomic_DNA.
DR RefSeq; WP_020214747.1; NZ_KB899976.1.
DR AlphaFoldDB; A0A0A2MCJ5; -.
DR STRING; 1121895.GCA_000378485_03573; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 1046984at2; -.
DR Proteomes; UP000030152; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030152};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..534
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 559..676
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 708..804
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 608
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 747
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 804 AA; 90765 MW; A3FA638870842355 CRC64;
MVQRPKALKF KVVAGYLLLF ATAVISVWFV YTEILKIARP VQNAGDNNKI VRISNTIASL
YASEAIGRNS ILTGDAKDLR HYNRLTDSIS REIDSIKKEV DPAQVQKLDS VQMLLSRKKN
SIAEIIQYRK TYTADNTFTK AIYGINIARD SIWTAIKPVK MTKVYEWRKV ANALLTPKQL
DSLSKLPVSN DSLVMAFENV INRLAIKDNK LKDQLYRREQ KMLEENRLIS DQLRFTLASV
ENEFVQKTYK NIYASQSALA NTVKTMAWVG AVTLFFLIVF AYIIISDLTT QQNYRKKLEV
LNLENEELLR SKSMLMATVT HDLQTPLGSI IGFHDLIKKL GVTPKQSHYL ANIKESANYI
LKLVNDLLDF SRLENNRITI EKSGFNMKHV IEAACRSLEP MAFDKNVELT WDIEEELNAN
FTSDPYRIKQ VLTNLISNAL KFTHEGSVEI TAKIEGNTII ISVLDTGIGI AKENHSAVFK
EFTQAHHGIE KKFGGTGLGL TISKKIIELL DGTISLESQE GQGSIFTITL PAIPAKNDEI
ASNTTLAKPN MYNLLKGKKI LMVDDDNVQL LLMKELFMHY PVTVVTEINS ASALHLIENE
HFDVLLTDIQ MPIMDGFELV KQIRQHSNTA IANMPAIALS GKRDLVPQDY IVRGFTAHHP
KPIQIEQLLE LVAGIFSENG VFDSNLLHLS GNDTLYSLKS LLQFTHNDPE SLNTILETFI
ESARDNCEVL QDAAIADDMD MVAQTAHKMI PMLRQMEVYS IVEKLLPLED RTITFNTGEL
KLYTDDICLR IDELCTKLET EMVK
//
