ID Q1LBA7_CUPMC Unreviewed; 1040 AA.
AC Q1LBA7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=bvgS1 {ECO:0000313|EMBL:ABF12569.1};
GN OrderedLocusNames=Rmet_5710 {ECO:0000313|EMBL:ABF12569.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF12569.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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};
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DR EMBL; CP000353; ABF12569.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1LBA7; -.
DR KEGG; rme:Rmet_5710; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_4; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABF12569.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:ABF12569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:ABF12569.1}.
FT DOMAIN 578..634
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 652..873
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 898..1015
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 281..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 947
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1040 AA; 112351 MW; 3D91A65609E6BE2D CRC64;
MLLRIGVMAN GLPPFDLVGI DGNYEGISAD YLAMIASTLH AKVEVRAYAT RDAALHDLSR
DAIDVVATDP GQTEPAQGAI GFTPNQIIEI ATRTTAHKLV GNQTLGYVNG QLDPQAILAA
YPGRKLQAYA TLLDALTQLS LGADVVLLSN ATAASYITAQ YGIPNLVAVN VSRLSVGDLS
FLVRDPALRA RFDAAIRAIP KPTRLAISTH WVPTALMPHF DKALNLTTEE SAWIAAHPVA
RYRATNDRVP FVFSDEHGES VGLSVQVLGK IEERTGLRFE PVSADGNSDP DHATTPTIQP
IVPVDGPSER TDGLTITEPY FQGYWAIVAH VRQHGINNIL DLAGKRVAVV LPNPIIDRLR
ATVPLQVVKA ASYRDAYRMV ATGIADATLG NMMTANYLIR ESYPEALRIV APISGTPLNV
GIGVPADEPM LLAILNKALL SLSREDINAL RLRWSEPSSI AGSTETLPSW AWFSLSAGLV
LLAISLLWSQ SLRQQIQRRR RMEAVLHEQL AFQTSILDAI PQPIYLRDID LRLMTCNAAF
ERALGCGRKQ MRGRTIDQMP LKLGDVPLSM QTYRKVLATG EAATLDRTLM IEGKERIVLN
WVEPLRNATG GVVGIIGGWI DMTERQQMVT ELASAKDRAE AANRAKSAFL ASISHEIRTP
MNAILGMLEL TLQDKRLPDD DRLQVETAQE SAKSLIGLID DILDASKMEA GKFVLTPQPA
PLRQLIGDVT SLFGLAASRK GVQLEAIVDD AVAPCHMVDP LRFKQVLNNL VSNAVRFTDR
GSVVIRLGAT NLTPDCQSLT FSVSDTGTGI PEDGLKKLFQ PFTQIGDTKR SAGGTGLGLS
ICQRLVTKMH GTIGITSEVG KGTTVTATIE LPIAAEIAPV LQSEQQNQPA SKPGKALRVL
IVDDHAPNRI LLQRQLEKLG HRAFTASDGC EALEKLTDAT FDLIICDYSM PNMDGPTLTR
TIRSSDLPYR TLPILGYTAS AQPEIRAHAI ECGMDAVMIK PVDMATLETT LAANVNRRAH
PGLPGLALAL APCGKSALTA
//
