ID A0A0B8P3I8_9VIBR Unreviewed; 603 AA.
AC A0A0B8P3I8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM19231_2658 {ECO:0000313|EMBL:GAM57539.1};
OS Vibrio ishigakensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM57539.1, ECO:0000313|Proteomes:UP000031671};
RN [1] {ECO:0000313|EMBL:GAM57539.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM57539.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (JAN-2015) 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:GAM57539.1}.
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DR EMBL; BBRZ01000057; GAM57539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8P3I8; -.
DR Proteomes; UP000031671; 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; 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:GAM57539.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031671};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:GAM57539.1};
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..603
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002122844"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..601
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 603 AA; 67712 MW; 556AF5D531B61365 CRC64;
MKKVRIFQTI LLVLLSLMSM FSQAQTSSVT QSGQTLEQKT QVDVGVLAIR GHLYAKSRWQ
PTIDWLNQII PEAHFVLHLL DLDGMSEAVK NQNMSFVLTN PGQAVRLGRQ YSLSWIATLS
NRNGQNINAS IGSALVVRAD SSYQSLQDVS GHPMAAVSER AFGGYLTLRY EAIQQGIDPN
TFYAEANFLG FPVDANLYQL RDGYVDAAVV PACLLEQMGR EGLLDVDKFR VLNAESSAEE
SCQVSTTLYP NWSLAKTGKG SDELAKKMSQ SLLSMKSDNP AAIAAKASGW APPVSLLSID
KLYQAMDLHP LQQPWWQEGL RWLRTHQEWG WALFLFVIFL NIYHFWLEYR FSKSKRELEL
TLQRLKAKSE MLEHSQRLMI VSELGSSIAH EINQPLAAIR NYSEGGLLRL QKERPHQDII
PVMTKIQAQV ERADAIVQRL RNLIKKRSVE MSETDLEQLI SDTVELLDFR LQKQSIDLIR
GQQGTARFIE VDPVGIQQVL VNVINNAIDA CVARADEDDY QAEIVLYTNY QQGQVEIEIR
DNGTGLTHDK PTEAFVSTKS DGLGLGLSIC RDVMEIHHGE FIIKSVEPKG CMVTLSLPFT
ADE
//
