ID A0A2A9F5N0_9VIBR Unreviewed; 606 AA.
AC A0A2A9F5N0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ATG66_2893 {ECO:0000313|EMBL:PFG45810.1};
OS Vibrio sp. ES.051.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761909 {ECO:0000313|EMBL:PFG45810.1, ECO:0000313|Proteomes:UP000223114};
RN [1] {ECO:0000313|EMBL:PFG45810.1, ECO:0000313|Proteomes:UP000223114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES.051 {ECO:0000313|EMBL:PFG45810.1,
RC ECO:0000313|Proteomes:UP000223114};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
RL Submitted (OCT-2017) 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:PFG45810.1}.
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DR EMBL; PDJL01000005; PFG45810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9F5N0; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000223114; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PFG45810.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PFG45810.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..606
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012134302"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 384..601
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 606 AA; 67904 MW; BA8350522F95D93F CRC64;
MKNAPPLLQF LILCLAAFSL VAQATSTIQG PQHDVKPQAD IGVLAIRGHL YAEQRWQPTI
DWLNQQITDV HFVLHPLNLD EMGEAVKFQS MDFILTNPGQ AVRLGRQYAL SWMATLTSRA
PKNSNYGIGS ALVVRANSSY QSLQDVMGLP VAAVSEKAFG GYLTLRYQIV EMGLDPNDFF
ADVRYLGFPI DANLYQLRDG NVQAAVVPAC LLEQMQREGL LQPDGFRVLN PQSSERSSCA
VSTSLYPNWS FAKTERGASL LAKRVAQQLL AMPPEHPAII AAGASGWTSP VSLLTIDKLY
QALDLHPLQQ PWWQDALRWL RTHQEWAWAL FIFVIVLNAY HFWLEYRFSK SKQALEQTSL
RLKEKSEQLE HSQRVAIVGE IGSSLAHELN QPLAAIRNYS EGGLLRLAKK RPHQDIVPVL
EKIQGQVERA DAIIQRLRNL IRKRSVEKAP CNMDVLIEDT IELLHFRMQK QNVSMVTTTE
GKTRPLLADV VGVQQVLVNV ISNAIDACVD FQEKYHMSDY QGKIALHTDY QAKRLCIRVL
DNGTGLEQDN PTQAFVSSKQ EGLGLGLTIC RDVMEMHGGE LVIQSAKPHG CLVELVFPYQ
TEGRQP
//
