ID A0A517VAH3_9BACT Unreviewed; 2453 AA. AC A0A517VAH3; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. DE SubName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ {ECO:0000313|EMBL:QDT89998.1}; DE EC=2.7.13.3 {ECO:0000313|EMBL:QDT89998.1}; GN Name=luxQ_2 {ECO:0000313|EMBL:QDT89998.1}; GN ORFNames=Pan161_16310 {ECO:0000313|EMBL:QDT89998.1}; OS Planctomycetes bacterium Pan161. OC Bacteria; Planctomycetes. OX NCBI_TaxID=2527971 {ECO:0000313|EMBL:QDT89998.1, ECO:0000313|Proteomes:UP000316855}; RN [1] {ECO:0000313|EMBL:QDT89998.1, ECO:0000313|Proteomes:UP000316855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pan161 {ECO:0000313|EMBL:QDT89998.1, RC ECO:0000313|Proteomes:UP000316855}; RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., RA Rivas-Marin E., Kohn T., Peeters S.H., Heuer A., Rast P., RA Oberbeckmann S., Bunk B., Jeske O., Meyerdierks A., Storesund J.E., RA Kallscheuer N., Luecker S., Lage O.M., Pohl T., Merkel B.J., RA Hornburger P., Mueller R.-W., Bruemmer F., Labrenz M., Spormann A.M., RA Op den Camp H., Overmann J., Amann R., Jetten M.S.M., Mascher T., RA Medema M.H., Devos D.P., Kaster A.-K., Ovreas L., Rohde M., RA Galperin M.Y., Jogler C.; RT "Deep-cultivation of Planctomycetes and their phenomic and genomic RT characterization uncovers novel biology."; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal CC transduction system that modulates chemotaxis in response to CC various stimuli. Catalyzes the demethylation of specific CC methylglutamate residues introduced into the chemoreceptors CC (methyl-accepting chemotaxis proteins or MCP) by CheR. Also CC mediates the irreversible deamidation of specific glutamine CC residues to glutamic acid. {ECO:0000256|SAAS:SAAS01100814}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + CC NH4(+); Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA- CC COMP:10208, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30011; EC=3.5.1.44; CC Evidence={ECO:0000256|SAAS:SAAS01116312}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L- CC glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA- CC COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, CC ChEBI:CHEBI:82795; EC=3.1.1.61; CC Evidence={ECO:0000256|SAAS:SAAS01130167}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00132521}. CC -!- SIMILARITY: Belongs to the CheB family. CC {ECO:0000256|SAAS:SAAS01100824}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP036343; QDT89998.1; -; Genomic_DNA. DR Proteomes; UP000316855; Chromosome. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 6. DR CDD; cd00156; REC; 1. DR Gene3D; 3.30.450.40; -; 2. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.180; -; 1. DR InterPro; IPR035909; CheB_C. DR InterPro; IPR022642; CheR_C. DR InterPro; IPR000780; CheR_MeTrfase. DR InterPro; IPR022641; CheR_N. 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; IPR013655; PAS_fold_3. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF01339; CheB_methylest; 1. DR Pfam; PF01739; CheR; 1. DR Pfam; PF03705; CheR_N; 1. DR Pfam; PF01590; GAF; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF08447; PAS_3; 5. DR Pfam; PF08448; PAS_4; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00996; CHERMTFRASE. DR SMART; SM00065; GAF; 2. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00138; MeTrc; 1. DR SMART; SM00086; PAC; 5. DR SMART; SM00091; PAS; 9. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF52738; SSF52738; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF55785; SSF55785; 7. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR00229; sensory_box; 6. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50123; CHER; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50113; PAC; 5. DR PROSITE; PS50112; PAS; 6. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050, KW ECO:0000256|SAAS:SAAS00706681}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000316855}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00132526}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050, KW ECO:0000256|SAAS:SAAS00706700}; Kinase {ECO:0000313|EMBL:QDT89998.1}; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}; KW Transferase {ECO:0000313|EMBL:QDT89998.1}. FT DOMAIN 14 197 CheB-type methylesterase. FT {ECO:0000259|PROSITE:PS50122}. FT DOMAIN 219 477 CheR-type methyltransferase. FT {ECO:0000259|PROSITE:PS50123}. FT DOMAIN 826 896 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 899 951 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 952 1024 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 1250 1295 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 1383 1453 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 1460 1510 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 1676 1746 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 1749 1801 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 1802 1874 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 1877 1929 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 2008 2063 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 2081 2297 Histidine kinase. {ECO:0000259|PROSITE: FT PS50109}. FT DOMAIN 2327 2446 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT COILED 647 709 {ECO:0000256|SAM:Coils}. FT COILED 935 955 {ECO:0000256|SAM:Coils}. FT COILED 1666 1686 {ECO:0000256|SAM:Coils}. FT COILED 2054 2074 {ECO:0000256|SAM:Coils}. FT ACT_SITE 20 20 {ECO:0000256|PROSITE-ProRule:PRU00050}. FT ACT_SITE 47 47 {ECO:0000256|PROSITE-ProRule:PRU00050}. FT ACT_SITE 139 139 {ECO:0000256|PROSITE-ProRule:PRU00050}. FT MOD_RES 2381 2381 4-aspartylphosphate. FT {ECO:0000256|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 2453 AA; 277421 MW; D537E904D4180473 CRC64; MKQNRQQNKN QPIIVGVGSS AGGLEAFGTL LEALQDAPGL ALVYVQHLDP ESKPVLMELL EKYTSLEVIV LKESTRLCAG KLYICPPQGL LEIKNGLINL SRNETDLHPS HNIDHFFHSL ADDQGEQAVG VVLSGAGSDG TLGLKAISDS GGLTFAQDPK SAKYDSMPRS AATTGVADHV LPPDAIASEL LNYARHLQKL NTSESLTRLQ DQIVDAIPQI TATLLKKTEH NFQHYKTSTL SRRIQRRMQV LKSSNVKEYL AYLQENEEET QALFRELLIG VTEFFRDPQA FDNLAGEVLP RLFENRSSDD CVRIWVAGCA NGSEAYTIAI LCREVMDRLK SPPQLQIFAT DIDERALQVA RAGIYPVGIE DQVSSERLKR FFIRRGKRYE VIREIRELVL FSVHNLISDP PFSRLDLISC RNLLIYLGPH LQKKLIPLFH YALRPSGYLL LGPSENITSH GELFRTIDSK FRISQRKGTA VESASTVPLI QSKLHLKSSL ERQPDAKVDL RNLRQRILLD EFAPKSCVID ESGQILNADA DMEKFLTLGE GDFQNNIVKM AAKGLRVGLR SALNEAIKKR RKVQQEHLRI RKGDQVQEVM ITVQPMPRLG EDEGLFMVVF HEVGLPVKKE ASEESLSGSV PHADAIIAQL DYELQSTRDE LEKSLQEMDV AHEEMKSTNE ELLSMNEELQ SANEELETSK EEITAVSNSV ARTNSDLENL LRSTQIATVF LDDELLIRSF TPAITEIYGL LNSDIGRPLE RFVPLVKEMP PLPDPHKLQQ GSPVEHTVIA VSGKIYIRRV LPYQSHSGKN EGIVVTFIDV SELHNSQELF QLLIDASSQI VWMTDAAGIV VEDSPSWREF TGQTYEEWKG TGWLNVVHQD DQQATIQAWQ SAVANVETFS VEYRLWNREG EWRWVHARGV PQKNRDGSIV RWVGMNNDIT EQKEAQREIQ ESRRQLQLGV EIANLGLGRV DYASDRITLT PEAAAIYGLG YQEILITRNE MLDLYHPEDR QAAADQIQAC IQECGDGRCD LEHRLVLPSG EIRWISARKQ IYFDRSLDPA VPVYATLVAQ DITISKREEL NLAFLSDLQT QLIPLSSVKD LMEVATRETA KYLDLFRCLI VEFDENADYA DIRFEHHVKS VPSIVGKHRV RDFHTENERQ KLLAGQQFFL SDTEHQIQDA QIAGKFREIG VGAYCNSAYV TPHGIKFVIS AVKREAYQWR PDELKLLQEI TNRLCIRFER ARAEAELVDR EAHLRRVINN QLGLVGVIDR DGRLLEVDDD SMKIAGLTRE DVIGKHFAEC AWWTYDEAVS QKMRESMAKS FAGEVVRYDV PLFAAGLGGP ERRLMIDFMM APVFGKNGEV EYLIPSGVDI SERVEVENLH KETAARLESM FNSAVDGMIT INTDGNIASI NPAAQELFGY ELEELQGQNV KMLMPEPWRS AQDSYLNAYL TTGQAKIIGS KKEFRGLRKD GSTFAMELTV SEALMHGEVM FVGTVRDISE RKQRELNLAF IDELQQLLGT PLITEEIMQQ TCARIADFLG LSRCLLIELD EEAEIASVVY EFHESGLSSI SGRHTITNFL GEEEREPLLA GQPILINNTQ NQDRKSKTAK NFASIQTGAI LSIPFVSDKR LKFALSICKQ QPYHWQTGEI DLLQELAPRI FVRLERARAE AALRESESRF RDLADNMSQF AWMADEKGFI FWYNQRWFEY TGTTLEEMQG WGWKKVHHPE HVDRVVKRIQ HSWDTGEVWE DTFPLRSKEG EYRWFLSRAV PIRDATGKIL RWFGTNTDIT STREQDQRVR ASEARLRLAM QAANLSLWQW DVVKDIIFWS YDNQNLSSIH PEDSENGLQQ FLNLVHRSDR ESVENNLRNC LSTGKPFRAE FRTRQAENSY AWVLSTAYLT TDSSDNSTLM VGVNLDITER KKSELAIKLS EERLRNAAES AGFGMLHIDL IEETTAYSPE MKRMLGLPEK TDKKLKFGEV PDWIHPKDRS AYLRHLQEAA VLPEGGNQSL DHRIIRPEGE IRWVRLHARP VFTGKGSRRK PTQLIGTLLD ITSQRQFEQS LKEARQMAEA ANESKSAFLA NMSHEIRTPM TAIMGYIDLI DDLIDHKIAT AYLSTVRRNG EFLLDIINDI LDLSKIEAGK LDIIRERFSP HQLLEDVCSI MDVRAAENRL ELEIFYQGMI PAEIESDPKR LKQILINLVG NAIKFTMEGS VNIFVSCQNH QLQFVIVDTG IGITSRQQKR LFRPFSQGDH TVNREFGGTG LGLAISQRLA NMLGGEICVE SEKGKGSKFT VTIATGDISG VKMIQPLTTG EAKETPKEET EIVLDCHVLV VDDRRDIRFL SKRFLTLAGA TVTEAVDGEQ AIAVVTAAMQ KGQLFDLILL DMQMPKLDGY ETARLLRKLG FTAPIIALTA DAMQGDMSRC IECGCNDYLS KPIDKNLLLQ TIKRYIGPDE NVT //