ID A0A171KX68_9BURK Unreviewed; 620 AA.
AC A0A171KX68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=AAV32_02925 {ECO:0000313|EMBL:KKO73485.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO73485.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO73485.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO73485.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-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};
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:KKO73485.1}.
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DR EMBL; LBNE01000001; KKO73485.1; -; Genomic_DNA.
DR RefSeq; WP_068367801.1; NZ_VZPC01000001.1.
DR AlphaFoldDB; A0A171KX68; -.
DR STRING; 206506.AAV32_02925; -.
DR GeneID; 73000097; -.
DR PATRIC; fig|206506.3.peg.643; -.
DR Proteomes; UP000078084; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.250.3020; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PIRSF; PIRSF036431; STHK_DctB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KKO73485.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000078084};
KW Transferase {ECO:0000313|EMBL:KKO73485.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 319..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..611
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 345..383
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 620 AA; 66506 MW; F6D14029CF87E68D CRC64;
MPVSRFFRRL GLLLPGIALL AALAGWAGYR HSLGVDLDAL QRAGQGRLAL YAASLERQID
KYAFLPATLA LERDVSLLVA RRPVDTHDPI LGLDPEPGPG PELAHAVNRF LERLNQLAGT
RVIYILDKQG QVQATSNWQQ ADSFLGEDLS YRDYFREAAA GRAGRFFGVG TTRGDPGYYL
SSPLYEDGEV AGVAVVKVGL EQLEQSWSKA EVPVLVSDAN GIVILASTPE WKFTALRPLS
DADRERLRAS LQYFDQPLDP LGLGDAGGLP GGTHLVSLPA AEPRQGGARR VPPYLAQEQA
LDGTGWTLTV LSPAGQLAWM AWTRAALAAA ATALVCILLL LWQQRRAYLR ERLQAREALQ
RAHDELELKV EERTRNLRAA QDELVHAGKM AVIGQLSAEL AHELSQPLAA LRTLSGNAGR
FMERGDLDAA RGNLDRIGTL VDTMGGLTSR LKLFARKSDG APQPVDVRRT IDNALFLLEP
RLRQVGAGMR MMVAGGVTAL CDANRLEQVL VNLIGNALDA VEGHASPAVR ISARRDGERV
RIEVADNGPG LPEEVLAHLF EPFFTTKEAG RGLGLGLAIS AGIVRDFGGT LSAAAAASGG
AMFVVDLPAA QAIAAKEGAL
//
