ID A0A1Q8YA37_9BURK Unreviewed; 1029 AA. AC A0A1Q8YA37; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 02-JUN-2021, entry version 17. DE SubName: Full=MCP methyltransferase/methylesterase, CheR/CheB with PAS/PAC sensor {ECO:0000313|EMBL:OLP04874.1}; GN ORFNames=BLL52_3690 {ECO:0000313|EMBL:OLP04874.1}; OS Rhodoferax antarcticus ANT.BR. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP04874.1, ECO:0000313|Proteomes:UP000185911}; RN [1] {ECO:0000313|EMBL:OLP04874.1, ECO:0000313|Proteomes:UP000185911} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP04874.1, RC ECO:0000313|Proteomes:UP000185911}; RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M., RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J., RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J., RA Sattley M.; RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple RT nonsulfur bacterium from an Antarctic microbial mat."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. 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:OLP04874.1}. 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; MSYM01000018; OLP04874.1; -; Genomic_DNA. DR RefSeq; WP_075588019.1; NZ_MSYM01000018.1. DR EnsemblBacteria; OLP04874; OLP04874; BLL52_3690. DR Proteomes; UP000185911; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd00130; PAS; 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; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013656; PAS_4. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase. DR Pfam; PF01339; CheB_methylest; 1. DR Pfam; PF01739; CheR; 1. DR Pfam; PF03705; CheR_N; 1. DR Pfam; PF08448; PAS_4; 1. DR PRINTS; PR00996; CHERMTFRASE. DR SMART; SM00138; MeTrc; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF52738; SSF52738; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF55785; SSF55785; 2. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50123; CHER; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050}; KW Methyltransferase {ECO:0000313|EMBL:OLP04874.1}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000185911}; KW Transferase {ECO:0000313|EMBL:OLP04874.1}. FT DOMAIN 32..223 FT /note="CheB-type methylesterase" FT /evidence="ECO:0000259|PROSITE:PS50122" FT DOMAIN 230..508 FT /note="CheR-type methyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50123" FT DOMAIN 859..909 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 912..982 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 725..754 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..26 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 738..753 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 44 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 73 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050" FT ACT_SITE 165 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050" SQ SEQUENCE 1029 AA; 112713 MW; DDC270C23F217E96 CRC64; MTKKIPGPSA KPPKTSPPAP PATPPTPVAT TALESFPIVG IGASAGGLAA FQAFFSGIPT GKAPGMAFVL VQHLAPDHKS LLAELLRRYT PMPVFEVEDT MVVQPNCVYV IPPKHDMALL NGCLQLLDPG APRSQHLPID FFFKSLAADQ RERAIGIVLS GTGSDGTLGA RAIKDAGGMV MVQTPDAAEF DGMPRSAVAT GLVDYQLKAN ELPAQLIAFL KYAYGKFSPN ADKPVLINDN ALKRIFVLLR THTKHDFSQY KPSTIHRRIE RRMAVHQISQ VDDYVRYLQQ NTEEAEALFR DLLIGVTNFF RDPEAFEALE HQVIPLLFAG KPTIGGVVRI WVAGCSTGEE AYSIAILLQE YMEEVKQSYT VQLFATDIDS RAVAIARAGL YPPGIAADLT PLRLARFFTE EPNGGGYRIH KSLRDMLVYS EQDLTRDPPF SRLDLITCRN LLIYLNADLQ KRLIPLFHYA LNPQGLLFLG TSEGIGDALV LFSTLDRKAK IFQRKNAEPG SQRLPSRFYP PLSGLEAAQP RALDRDVSHS KLSLRELTEQ ALLAQVAPAA ALINTLGDIL YLHGRTGMYL EPAPGEVGVP NILKMAREGL RPALSNSLHR AMASQAPVHT PGLRVKTNGH FTRVNLCVRP VSSSPSAPAS RAETHDSLAK APQDVQLYLV MLEEAPDQLP EANAPLLLAG AAAPELAEPQ NADTAAQLAA LRNELRAKDE YLRSTHEELE TSNEELKSSN EEMQSINEEL QSTNEELETS KEELQSLNEE LSTVNHELNL KVDDLSHLNN DMNNLLAGTG IATVFVNIQL RILRFTPTAS KLINLIASDI GRPVGHIVSN LVGYRSLVAD AQAVLDTLAP KELQVQTIDG AWFTLRLRPY RTLDNVIEGV VITFSDISEL KSTEAALAKA NELTRLAVVV RDAFDAITMT DLEGRILAWN PAAERLYGWT EAQALQMTLR ERIPPELVDE AMQRLKQLSE GKVLALYPTQ RLTRSGKTVA VSLFATALIN AAGQVYAVTT TERLRTSDT //