ID A9BC70_PROM4 Unreviewed; 504 AA.
AC A9BC70;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=P9211_15011 {ECO:0000313|EMBL:ABX09432.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX09432.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX09432.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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};
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DR EMBL; CP000878; ABX09432.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BC70; -.
DR STRING; 93059.P9211_15011; -.
DR KEGG; pmj:P9211_15011; -.
DR eggNOG; COG3447; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_540647_0_0_3; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000000788; Chromosome.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR 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:ABX09432.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW Transferase {ECO:0000313|EMBL:ABX09432.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..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 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..504
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 504 AA; 55352 MW; 7DEE1D7DC9EB383E CRC64;
MLINYKLKKF VDLISINLAA ISGYFLLALL AKEAFAWQST AITLWPASGL ANALLISHGW
IALPGIAIGN FLGTAFDPNA GFSFQPFMLP VAIAAAAQAG FVRWMLIRKN LLNDPLTRIP
RLITFLLIIG PLGNWPAAAT FLSYRIANSG NLNINNFSLL DSNYVNGSFF WWLGDSLGSL
LLLPLLFLLL PFKRPIWLER RTYLLSPLLA MIALLITGSF LERMLLERID ITPQMLEPIQ
GLRLLSTFAW IVVALGVLGL ILQISGKYLE QEKLLSRSRL TGDAAGAVIH EIGQPLIRLR
LRLENIVKWH KKNSNIENKD FPFNKNITNE AEKSLQELNA VVVNTRSIQD LTLAGIRDTN
AANLADAIAM ASAQLRSDFD RLDQDLSVLI KQELPEVSSG QVQLQAAIRN LLSNASKAAG
EHGVIRINAG LMLGYVVCEI EDTGSGFAPS SMPDGRERIK SKTGGMGLGL MIVRRVIDDN
GGEIEFSSSK ELGGAKVRIW LKPS
//
