ID Q5V1K1_HALMA Unreviewed; 334 AA.
AC Q5V1K1;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=rrnAC1693 {ECO:0000313|EMBL:AAV46601.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV46601.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV46601.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809
RC {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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DR EMBL; AY596297; AAV46601.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5V1K1; -.
DR STRING; 272569.rrnAC1693; -.
DR PaxDb; 272569-rrnAC1693; -.
DR EnsemblBacteria; AAV46601; AAV46601; rrnAC1693.
DR KEGG; hma:rrnAC1693; -.
DR PATRIC; fig|272569.17.peg.2378; -.
DR eggNOG; arCOG02364; Archaea.
DR HOGENOM; CLU_000445_114_58_2; -.
DR Proteomes; UP000001169; Chromosome I.
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; IPR031623; HisKA_4TM.
DR PANTHER; PTHR44936:SF9; SENSOR HISTIDINE KINASE GLNK; 1.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF16926; HisKA_4TM; 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:AAV46601.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169};
KW Transferase {ECO:0000313|EMBL:AAV46601.1};
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 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..321
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 334 AA; 36714 MW; 292647E4A9A0E096 CRC64;
MSIVRPSPVD VVILGVGLTP ALALVAANYW LPVSGLSGDQ IWTAAEWCGL GVALFTVIKI
VVLLAPVPQS SMIPSILASG VAVGGFGGIL FGWLLELRRS RRRLAQSNEV LFRVLRHDLR
NDLNVALGHL GELQRETAER GRPESRAHVE QLSGTIDGII ATTEKARQIE FAFDADRRAQ
EPIDLVPCVR EQAKKITQST PEATVELDLP EQSRVYADWM LDTVLRNVIE NAVVHCEETP
TLYISVEEHG RTVFVHIGDN CPSIPQHERD VLNSGVETQL CHSKGVGLWL TTWIVESYGG
AVHLTTSDDG NTVTLELCGP TVLDEIRQTL REWP
//