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Database: UniProt
Entry: A0A316EH59_9BACT
LinkDB: A0A316EH59_9BACT
Original site: A0A316EH59_9BACT 
ID   A0A316EH59_9BACT        Unreviewed;       446 AA.
AC   A0A316EH59;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=LV89_00602 {ECO:0000313|EMBL:PWK29048.1};
OS   Arcicella aurantiaca.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Arcicella.
OX   NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK29048.1, ECO:0000313|Proteomes:UP000245489};
RN   [1] {ECO:0000313|EMBL:PWK29048.1, ECO:0000313|Proteomes:UP000245489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK29048.1,
RC   ECO:0000313|Proteomes:UP000245489};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAY-2018) 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:PWK29048.1}.
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DR   EMBL; QGGO01000002; PWK29048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316EH59; -.
DR   Proteomes; UP000245489; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:PWK29048.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245489};
KW   Transferase {ECO:0000313|EMBL:PWK29048.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          226..446
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   446 AA;  51093 MW;  93627730F1D4F5BE CRC64;
     MLRFNRYEIS LTIRVVLLLA SITVAAFCIV MAKYSLLVFA ILLLVFQIFN FVQFINKTNI
     ELSQFIEAVR YRDFSLQFTE KNAPVSVRQL RRAFNQINST FKQLSSEREE QYQYLQKILE
     LVDTGILSYN QEGEVGWINE SFKRMMNVPY LRNISSLEKR DVVVYQVIMN LENGDSQLVK
     INQKQVLLAK TTFLNEDVET NLIAFQNVNE AIEDTEAQAY QKLLRVMTHE IMNSVAPIAS
     LAETIEKTLH HNGQANEKLN TENAQFDDIV LGISTIRKRS ENLLKFADTY RQLAKVSITS
     FSDFFVHDLF EGVEILLENQ IEQKNIEFDV VIKDFELTIE GDMVLVEQML INLIINAIDA
     VKNQENPKII LSTYRGQDER PVIEVRDNGI GMSPDLMDKI FVPFFTSKPN GSGIGLSLSK
     QIMTLHKGTI SVHSIEGEGT IFRLGF
//
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