ID A0A2A4BAA2_9SPHN Unreviewed; 748 AA.
AC A0A2A4BAA2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=COC42_01005 {ECO:0000313|EMBL:PCD04606.1};
OS Sphingomonas spermidinifaciens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141889 {ECO:0000313|EMBL:PCD04606.1, ECO:0000313|Proteomes:UP000218366};
RN [1] {ECO:0000313|EMBL:PCD04606.1, ECO:0000313|Proteomes:UP000218366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9NM-10 {ECO:0000313|EMBL:PCD04606.1,
RC ECO:0000313|Proteomes:UP000218366};
RA Feng G., Zhu H.;
RT "Sphingomonas spermidinifaciens 9NM-10, whole genome shotgun sequence.";
RL Submitted (SEP-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:PCD04606.1}.
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DR EMBL; NWMW01000001; PCD04606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4BAA2; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000218366; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF9; SENSOR PROTEIN RSTB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PCD04606.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000218366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..371
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 497..715
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 722..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 80793 MW; 169B34D24F22D463 CRC64;
MLSSEPRRRL SVTPLIELGV LAAAVAIGIA TYFIITADPT SPRPLTPPLV ALLMVANLVP
AVALLVLIGR RIAIKRAMAS AAGGQGRLHV RLVALFSVLA SVPMILVTIV ASMLFQYGVE
FWYSDRAKDM IERAATLADE SYREMTRWID GENIALGKDI QRVLAAGYPF DTPEFIATFE
QSVFQRSLAE SIVFTLAPDG EVLTYALLDP YERGLASSLS VADARAVLAG RPSVVIVSGE
RIQSIAPVPG TRYLVASSRV VGARELMERK QRAEGVVADY RALRERSRSL QLRFNLALLG
ISLFIVGLAV FAALAIADRL VRPVNDLVDA ARGVAGGNFD ARVSQPKRMD EVGTLASAFN
TMTERLKEQT GALVAANAES EGRRALIEAV MSGVSAGIVS IGAERTVRLI NSSAAHLLEI
GEDDAIGRPL TEVAPELDAL LASDQREAVV QVARGGEART LAVKITRDAA GPILTFDDIT
QQLADQRRAA WADVARRIAH EIKNPLTPIQ LAAERLQRRY GKSIEPSDTT FSRLTETIVR
QVGDLRRMVD EFSSFARMPK PVFRRESLVD IARQAMFLHE VGHPGIAFRL DTDPDAPVSL
VCDRRQIGQA LTNVIKNAAE AIEARPAADN LPQGEIVMTL AKSNGRVTLS VADNGVGLPL
ERDRIVEPYM TTRSRGTGLG LAIVKKIAEE HLGAVSFADR PGGGTIVTLA FDARALEPLA
VPEDAEATPA STDDDRLHML TRTRNPNS
//