ID A0A1S8FGS2_9BURK Unreviewed; 678 AA.
AC A0A1S8FGS2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B0B52_13410 {ECO:0000313|EMBL:OOG40493.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG40493.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG40493.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG40493.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OOG40493.1}.
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DR EMBL; MUNO01000024; OOG40493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FGS2; -.
DR STRING; 1944133.B0B52_13410; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000218978; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR029095; NarX-like_N.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13675; PilJ; 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 SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..480
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 436..678
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 420
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 678 AA; 74935 MW; 721F53B917EAA00C CRC64;
MKSSLGLGKY RDLLFAILLF IVLDLGILFF NFFASLQLER DASRINTAGE LRMLTQQITK
SLLTLQVEKK GELPIQTSMA QLTQGTGAFV EGLAGLKNAM SRDAEFTIFG LNPDDLRDTL
RKLEREWLPL KESIDPVIAA QDPTLEDTDI AATKAVARNI RLMALSDDLA TGVEAAARTK
TERMRQIQVA AIVLALINFV YIVFKFLRRL NASDRVADAA RQETDDILKT VSEGLLLVRS
DGSVGTQLSA SVHKLFMREI RPGEDFRQLL RSVLTPERAE EAQSYLELLF DPKVKPALLT
QLDPLKDVEV TAPGASGAVR FLTFQITQLR EAGRIKELLV TVFDVTRKVQ LERELAATQE
AAKSDVEDLI RVLEQEPLLL QEFLLGARAR LADLNQSMRT VGRRPEAYRA LVDDAARLIH
GIKGEGAALS LTAIARQCHE MENALAPLLK RRDLSGEDLI PIVFELSKVQ DQAERLHRVF
ARIGQASPAV QQDEPRLLDA MVGNLRSLSE RVALSLGKQV RLTAYVNETV LPAGVEQVLR
EALPQLVRNA VVHGIELPLE RQKLSKPPVG ELRLDIGRAE DGAIQVTLSD DGRGIMVPEV
RQRVAQLRTD ATQLTDSQVL GFIFDPHFST ASEVTEHAGR GVGLSLVKQI AEKAGAKLRV
MTRPNVSTQF VLKFGVVS
//
