ID F3LIB4_9GAMM Unreviewed; 903 AA.
AC F3LIB4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=IMCC1989_1277 {ECO:0000313|EMBL:EGG93371.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG93371.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG93371.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG93371.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(2011).
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:EGG93371.1}.
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DR EMBL; AEVK01000217; EGG93371.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LIB4; -.
DR Proteomes; UP000010300; 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 CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGG93371.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010300};
KW Transferase {ECO:0000313|EMBL:EGG93371.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..327
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 483..534
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 535..607
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 610..662
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 680..897
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 372..399
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 903 AA; 101727 MW; 9539E22D03E68950 CRC64;
MNDSFDRLQE KQSTQSAQDF SLKLSTYLQN RLSVLNDLAS SALITNTVLL GEKNNPALAD
FFHVARLLGE DPSLTLVDFN GNVLLTEVND NTDSYRWVLP LLEASLSDVS VVQPSEIVNF
ITADSAGVAL EIPLFELAVP VIYGKSRDGV LIARIDASPS VVYRDGLIKS GVSEVQYSKQ
NNMISSDVDS IALPDKKTVF IDTYEISFSH IVSQENVQKS KQELWVRLSV GAFISALVMC
FGLFFLGRKS ILQPYIKLAT LQNAVSKAVE GISFIDPSGC YVSLNQAYAA PAGYLPEELE
GKPWSVTVHP DDMPMLNEAY QQMLDEGSVV AEARGVRKDG STFYKQVTMI TQYNGDGEMI
GHHCFLKDIT ERKEEEAGRE ELIQALARTN DNLIDSQEKI LSGDKKLRTV LNFQSVVFDN
VPDMLFVKDT EFRIVQANEA FLNVYPENMR SSVIGSTCLE GYKEDEREEF LFFDRIAFDK
GFSETEESIL FPDGKYRTLL TKKVRFKDEQ GEVFILGVAS DITQIKQAQQ ELLKSEQRYE
VAVKGSSVGL WDFDVLTGEL YWSDRFKQIV GVADSDFTGT LEEFAGRLHP EDEERVLSQF
NLHLSNKAPY NVEYRFRKED GDYVWVHAEG QALWNEEGQP IRVAGSVEDI TKRKSSEIER
EKLIDKLAES NEGLEHFAFV CSHDLQEPLR IIRSFSERLQ KHMGDSLDGD DKAQLYFKFI
VDGAARAQVL IADILTYSRV DNDTQPLEEV SPETLVEAVK QHLQVGFEDD KRQVIYSDLP
LVVGNKTQIY QLLQNLINNG LKYQPADRDP SVYVSAVDDG QGYWQFTVKD NGIGIEPRYQ
KQIFDVFKRL HGQGEYSGTG VGLAICKKVV ERHGGRLWVE SEKEQGASFH FTLPKKAPIE
IES
//
