ID A0A0C9LZU4_SPHPI Unreviewed; 1110 AA.
AC A0A0C9LZU4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SP6_07_01360 {ECO:0000313|EMBL:GAN12350.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12350.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN12350.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12350.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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 -!- 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:GAN12350.1}.
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DR EMBL; BBJS01000007; GAN12350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LZU4; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16919; HATPase_CckA-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
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 Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 198..255
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 276..328
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 329..385
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 402..454
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 743..967
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 988..1104
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1038
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1110 AA; 123051 MW; F5F91479564507C5 CRC64;
MTPPNDQGPV PAWNEDARLA ALDRYAILDT GRDAAFDDVV RLIADVFEAP IAVVNFVAAD
RQWFKAEIGV GTDTLPLDAS LCRHAILQPG VFIVPDTLED ERFVHNPLVA GDPRLRFYAG
ALLETSDGLP IGTLCVLDTK PRPDGITERQ RFTLQLLARQ VMAQLDLRYE IAMREEHALR
LEAEIAGRNA ADQAHRESKR RLDAVLNNTR MAVFLMDEQQ QCVYANAAAE TLTGYSLAQM
KGRPLHNVVH HTRPDGSHYP LEECPIDRAF PERAQMDGEE LFVRPDGSFY PVRFTASPLL
DENEQPVGTI IEARDITASR ARDAALRESE ARFRNMADHA PVMMWVTDAD GNCTYLNRAW
YEFTGQSEDA AHGLGWLDAV HPDDKGWSGD MFLAANAARE AFRLEYRLRN RDGSYRWAID
AASPRFDAHG VFLGYIGSVI DINERREAEN ALRISEERYR TLFETIEVGF CIAEVLFDGD
QAVDYRFIEA NPAFEKQTGL LHAAGRTARE LVPGLEQFWF DRYGQVARSG EAARFESGSD
AMGRWFDVHA LRIGHPSANR IAILFNDVSA RRQAELQLRE INDTLELRVE EAVAERQLWA
DVIENTDALI AVVSSGFRYL ALNAAYAEEF ERIFGVRPKV GDHLPDLMAQ MPEHCEPVLA
IWRRALEGEN FSVVEEFGDP DRDRPYYELR FNALHDRMGR FVGAFQYAVD VSDRLRDQAR
LAEAEEQLRQ AQKMEAVGQL TGGIAHDFNN LLAGIIGSLE IIERRLSTGR TDGLDRFING
AQTSAQRAAA LTQRLLAFSR RQTLDPKPTD VNRLVFGMED LIRRTVGPAI KVEVVGAGGL
WPAKVDAAQL ESALLNLAIN ARDAMPMGGR LTIETANKWL DDRGARERQL PPGQYLSICV
TDSGTGIPKD IVDRIFDPFF TTKPIGQGTG LGLSMIHGFV RQSGGQVRVY SEEGHGTTMC
LYLPRFLGEV GEDQVPDEAI ADDGAGRTVL VIDDEATVRM LIVEVLEEAG YTAIEAEDGP
SGMKVLQSDI AIDLLITDVG LPGGMNGRQV ADAAREIRPD LKVLFVTGFA ENAAVGNGHL
SPGMAVVTKP FVMTELGNKI VEILETPIGA
//
