ID A0A127R213_9BURK Unreviewed; 1194 AA.
AC A0A127R213;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=bvgS {ECO:0000313|EMBL:AMP16333.1};
GN ORFNames=CPter291_4100 {ECO:0000313|EMBL:AMP16333.1};
OS Collimonas pratensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP16333.1, ECO:0000313|Proteomes:UP000074914};
RN [1] {ECO:0000313|EMBL:AMP16333.1, ECO:0000313|Proteomes:UP000074914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter291 {ECO:0000313|EMBL:AMP16333.1,
RC ECO:0000313|Proteomes:UP000074914};
RA Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT "Exploring the genomic traits of fungus-feeding bacterial genus
RT Collimonas.";
RL Submitted (NOV-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};
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DR EMBL; CP013236; AMP16333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127R213; -.
DR PATRIC; fig|279113.10.peg.4090; -.
DR Proteomes; UP000074914; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
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 InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
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; PF01627; Hpt; 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; SM00073; HPT; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 559..631
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 703..926
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 948..1064
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1092..1186
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 997
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1131
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1194 AA; 131593 MW; 5CA6C46DFAADB339 CRC64;
MLALDTDPSA ERLQIVERPL EQNLVFNLSG DDWRWLGKKR VLRVGTVGPD HPPFDFNDGH
QDFDGLTADY VALLAKHMGL IVEVVRYPTR EAANMALTRG SIDLLGNTLQ SDLSGQDFVL
SRPYAVNRAA IVVPIGKHKI ASKPGAALRI AVVPGYLSDQ DLHHLYPLAN FKPYPDTRLA
IAAVLDGHAD IFLGDAIGAS FLLHKGYFSV LQIDGFAPAS SRGVGFAVYK QNDVLLRILD
TLLQSIPEST HRAMLQRWGV GLDFRLTSTP LALTDAERRW IALHPKVRVA VTGLFAPITF
YKQNGQFDGL LADYLRLIEL RTGLDFEVVR YASIPDMLNA VREGQAQMVG ALIMSPERQA
DLTFAQPFLL NNLSLVTRSG DTRISYLSQL TGKKLAIQIG NPMIAQLRKE YPGIQLVLAD
QAISAFEKLD EGEVDAIIQT QIVSSYFMEG PFRGKLRFAG PVGDELARIA MGVRRSEPEL
RDVLNKVLRS IPPNEALMLT NRWREKNDAE PSSWDTYRWE IYQIAAGALL LILASLFWIA
YLRRQIAKRK LAERALGDQL AFMRAMIDDT PHPIYVRDLN ARLIECNRSY LEAMGGARDQ
VIGKLLPEST VFPPETAQEF HAMYLQTMQD GIPVFADRDM AFGERHLRIY HWTLPFKDTR
GKPAGLIGGW IDISEREQLI SALQLAKEEA DEASRAKSTF LATMSHEIRT PMNAIIGMLE
LVLKRGENGL WDRPSIKVAY DSAKTLLGLI GDILDIAKIE SGKLELVPER ANLRELVEAV
ARVFDGLARQ KGLTLRTFID ANAGAEVLID PMRFKQILSN LVSNAIKFTQ EGEVTIRLDV
ADEKEGRLAV QLQVSDTGSG IPQEEQAKLF APFVQASATR PRSAENGTGL GLAISRRLAQ
MMGGDIALQS ELGVGTQILV KFTVATVEPL DTPQLQATTV APKLGRLRVL VADDNVANRL
VLCQQLQYLG HDVESAEDGR EALQIWRAGS FDLVMTDCNM PVMSGYQLAR EIRNETEAPR
CVIWGYTANA QPEEIQRCKA AGMDDCLFKP IGLDDLQRRL TAGLPHNVAD AKPKPADSLF
DASSLEAMTG GNFALISRLA KELINSNRND SLLLIQRVTA ADWLAVGDVA HSIKGASTIV
GAQVLSEVAA ELESLCRDGA ADGDLRQAAS VVLAEITQLE QSLESWLLAE AGET
//
