ID A0A0S2K4B9_9GAMM Unreviewed; 587 AA.
AC A0A0S2K4B9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PP2015_2692 {ECO:0000313|EMBL:ALO43179.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43179.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO43179.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43179.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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};
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DR EMBL; CP013187; ALO43179.1; -; Genomic_DNA.
DR RefSeq; WP_058030856.1; NZ_PNBV01000009.1.
DR AlphaFoldDB; A0A0S2K4B9; -.
DR STRING; 161398.PP2015_2692; -.
DR KEGG; pphe:PP2015_2692; -.
DR PATRIC; fig|161398.10.peg.2749; -.
DR OrthoDB; 5638366at2; -.
DR Proteomes; UP000061457; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALO43179.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..243
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 348..579
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 224..339
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 587 AA; 66401 MW; 8810D8FAD7AE31E6 CRC64;
MLQKSLSKKL LTNVLSVYFL LTFLVTCGQV ITEYINTKNY IQNELTMLQK TFSRSLTRAI
WELNTKQTVT TAEGLLAIPM IEGIIVRDDS GEIISQLGRS LDIHELYSQQ LVQEEVIIED
TPSGLFGYTF PLIFEFSGRA TQVGDVTLFS SREVVLSRIM LSIYFLLGNA VVKTTFLIIL
FLIAFRKLLT EPLTDLTEQI EAFELNDDID GQRIDIGTTE RNELKVMEEA FNKLIDKVSD
YRNQLDDTQK ELLISNEKLD QHNLQLEQEV ARKTSNLSQA MMDLQQQKYE LEKQKLTLTE
EIDLRRQTEQ ELLTKQKELE RYLDELNMAQ ERLVGSEKMA ALGGLVAGIT HDINTPVGIG
VTATSFLQER LEQIEAAYKD KTLSPKALEE FINDAKQSTS LLTTNLDRAS ELVASFKQIA
VDQASEAVRN INLKQYLAEV IRSLHPKLKK TKHAINVECP EDLQLNLPAG AISQIFTNLI
MNSLIHGFEG IDQGEINIEI KNDNDDVVIH YKDNGRGVSQ TQLEKLFDPF FTTKRDQGGS
GLGTHITLNL VKQTLNGEIE VSSEEGKGLS YMIRFPKTLQ QSANMFD
//
