ID A0A0A7PE18_9SPHN Unreviewed; 598 AA.
AC A0A0A7PE18;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SKP52_06245 {ECO:0000313|EMBL:AJA08174.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA08174.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA08174.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA08174.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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}.
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DR EMBL; CP009122; AJA08174.1; -; Genomic_DNA.
DR RefSeq; WP_039572858.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PE18; -.
DR STRING; 1515612.SKP52_06245; -.
DR KEGG; sphk:SKP52_06245; -.
DR HOGENOM; CLU_000445_94_2_5; -.
DR Proteomes; UP000030907; Chromosome.
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 CDD; cd12914; PDC1_DGC_like; 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 Pfam; PF00512; HisKA; 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:AJA08174.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AJA08174.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 389..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 332..380
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 598 AA; 64712 MW; DAF7D5D8429BF3CF CRC64;
MPLKNDSTPV GPHTNRRRLF VAVAIGLAIL LVAALGLAHW AADRAGAQAD VEARQNARAH
ASLLESELQK FRLLPRVLTE FPDVRAALAD KSDAASRRLD RELEQLAART DATVIYVIDA
DGTTIAASNW RAPTSFVGEN YRFRPYFQGA MRDGEAELFA LGTVSGRPGL YLARRVDVGG
RQLGVIVLKV EFDKLEARWA DSAAATLVID AAGIIVMSSE PRWRFRSFVP ISAATQQRLR
ATRSYGDARL DPLPVERVDG GVRVGAELYR QADERVSFPG GTLRLLQPAA PARASANATA
RVAFLVLLIL VGAAIITLLR LVERQTLRQA AHDALEREVA ARTRDLRTAN DELRLASERQ
RETDRRYRAA REELAQASRL GSIGQITAGV AHEINQPIAA IRTFAENSLR YLERAEPDKA
RGNLDTIVAL TARVGAITNE LRNFARRKPT PLGPVAVQSA VDGTLLLIGD RLRAQGITLD
VDIENPATSV HADRVRLEQV LVNLLQNAAD AVHGEKEPRI ALHAHGSDPV HIDVCDNGPG
VPATLLPQLF TPFVTGRPDG LGLGLAIASD IMAEFGGALT LIPSPFGGAG FRLTLRLA
//
