ID Q92UP1_RHIME Unreviewed; 907 AA.
AC Q92UP1;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=Blue-light-activated histidine kinase {ECO:0000256|ARBA:ARBA00021740};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=exsG {ECO:0000313|EMBL:CAC49456.1};
GN ORFNames=SM_b20933 {ECO:0000313|EMBL:CAC49456.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB {ECO:0000313|EMBL:CAC49456.1,
OG ECO:0000313|Proteomes:UP000001976}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC49456.1, ECO:0000313|Proteomes:UP000001976};
RN [1] {ECO:0000313|EMBL:CAC49456.1, ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|EMBL:CAC49456.1,
RC ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorholter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puhler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2] {ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymB {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3] {ECO:0007829|PDB:3HCY}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 292-439.
RA Zhang R., Xu X., Cui H., Savchenko A., Edwards A., Joachimiak A.;
RT "The crystal structure of the domain of putative two-component sensor
RT histidine kinase protein from Sinorhizobium meliloti 1021.";
RL Submitted (MAY-2009) to the PDB data bank.
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; AL591985; CAC49456.1; -; Genomic_DNA.
DR PIR; H95973; H95973.
DR RefSeq; NP_437596.1; NC_003078.1.
DR RefSeq; WP_010975895.1; NC_003078.1.
DR PDB; 3HCY; X-ray; 2.80 A; A/B=292-439.
DR PDBsum; 3HCY; -.
DR AlphaFoldDB; Q92UP1; -.
DR SMR; Q92UP1; -.
DR EnsemblBacteria; CAC49456; CAC49456; SM_b20933.
DR GeneID; 61601015; -.
DR KEGG; sme:SM_b20933; -.
DR PATRIC; fig|266834.11.peg.5985; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_000445_114_57_5; -.
DR OMA; QGLVCTI; -.
DR OrthoDB; 341208at2; -.
DR EvolutionaryTrace; Q92UP1; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_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; IPR013655; PAS_fold_3.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR41523:SF8; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF07536; HWE_HK; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3HCY};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAC49456.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:CAC49456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 19..59
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 97..149
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 146..216
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 219..271
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 534..586
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 658..713
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 907 AA; 99620 MW; 9A65B0EDA8B5A5EC CRC64;
MHGAEILPKT TIDDVTTSDT PDYRAVLDAL AVPVYATDAE GIVTYCNAAA AAVAGREPEL
GKDRWCVSWQ LRRPDGSPLP HDECPMARTL KEGQPVRGEE VVAVRPDGAS VPLLPHPTPI
FDDTGALTGA VNVLMDLSGA KDMERSSRYL AAIVESSDDA IVAKNLDGII TSWNRGAQRL
FGYAAEEVIG ESITILIPPE RLSEEPGILE RIRRGELVDH FETKRRRKDG TLVDISLTVS
PVRDATGRII GASKIARDIT ETKSAAEALA ARFREQAALY RLTERVQRTK RIEEVYEATL
DAIQGALNCD RASILLFDEA GTMRFVAARG LSEHYQRAVD GHSPWITGAN EPEPIFVENV
DDAEFSRELK ESIVGEGIAA LGFFPLVTEG RLIGKFMTYY DRPHRFADSE IGMALTIARQ
LGFSIQRMRA EYARRQAEEQ LRRNEANERA RAAELAAIME AVPALIWIAR TPDCRVISGN
NSSYEILRLP HDSNLSMSAP PGEHPTNFRV FSEGRALSPE ELPVQRAARG EEVQNFEEEV
RFDDGSSRHI FGNATPLRDV TGEVVGAVAA AVDITGRKQA EEALQESERR LQLALDAGHM
GAWEWNLETG EVIWSPGLEA LHRIEPGSFG GTLADFKRDI HPDDLPLIER EMARAIETDG
DYHVVYRAQL PDGTIRWMEA FGQLSPRNGP KRRLTGVCMD ITERREAEAQ RNLLVAELSH
RVKNTLAIVG SIARQTFSTN PDAKAAHRSF DARIRALAQT HTRLAEASWS GVSLKTVLFD
ELSPYHDDSR TNVTLAGPPA MLPPKHALTL GMAAHELATN AAKHGALSVR SGKVDIEWMI
DVASERLRIC WSETGGPAVV APKHNGFGRL LLERVLASDL GGEVHLEFAP QGLVCTIDVP
YPRGAPG
//