ID A0A1A7QZ31_9FLAO Unreviewed; 1537 AA.
AC A0A1A7QZ31;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=LX77_03399 {ECO:0000313|EMBL:RAJ19769.1};
OS Gelidibacter algens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gelidibacter.
OX NCBI_TaxID=49280 {ECO:0000313|EMBL:RAJ19769.1, ECO:0000313|Proteomes:UP000248987};
RN [1] {ECO:0000313|EMBL:RAJ19769.1, ECO:0000313|Proteomes:UP000248987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12408 {ECO:0000313|EMBL:RAJ19769.1,
RC ECO:0000313|Proteomes:UP000248987};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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:RAJ19769.1}.
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; QLLQ01000019; RAJ19769.1; -; Genomic_DNA.
DR RefSeq; WP_066436696.1; NZ_QLLQ01000019.1.
DR STRING; 49280.A9996_14730; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000248987; 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:0000155; F:phosphorelay sensor kinase 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; cd02440; AdoMet_MTases; 1.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_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; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 3.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..197
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 220..471
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 958..1012
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1225..1278
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1307..1535
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 651..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 26
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1537 AA; 174537 MW; 18FD9A802888C529 CRC64;
MAKEKKNKTQ PPATKQNFPI VGIGASAGGL DAFKKLLPAI PESSGMAYVL VQHLDPSHES
MLPEILQRVT KVPVHEITED IHLAPDHIYI IPSNKILTST DGVLQLAPRD KNKVNLSIDI
FFTSLAEVHK ECAVGVVLSG TGSDGTLGLK AIKEHGGIGI AQDLKSAAYI SMPQSAVKAG
VVDFVLAPED IPAQLLQINS SYKANNVFED SEQVIEDDNE ETFEKILLLL HQRSGVDFTF
YKRPTFHRRI ARRIAIVDKN NISEYLSFLR ANDDEQDALF QDVLIPVTSF FRDPKTFKNL
RDTVFPDLFQ NKSTGDTIRV WSAGCSTGQE AFSLAICIAE FLGDKSTELK IQIFASDISE
KAIKKARSAI YTKAEVEKLS ESYLNKYFTK NNGGYEVNKR IRQMCVFAPH NFLKDPPFAK
MDLISCRNVL IYMDAFLQKK AFTTFHYALK ANGVLLLGKS ETVGASSDLF SPLVKNDKIY
SRKPVPGRFM HVATERREES MVTKDKTATK KVANLTDFRK SAEAIMISNS PASVVVNEQM
DIVHIHGDIT PFLQSPQGKP THNVLQMARE GLAFELRNAI HKAKTSEETV IKENIPVNTN
ARRSARAGTE SNNDVGQGKQ ALVTIEITPL TNTVDIHYLI QFQEKIIPSV QDNKKSSTGK
ASAAQKQNEN LEKELSQTRE DMRSITEDME AYNEELQSAN EELQSSNEEM QSLNEELETS
REELQSTNEE LIIINQELVD KQDQLHAARL YSDSIVSTIR HPLIVLDKDL CVKTANAAFY
KKFDVDEKNT EKKWFYEIQH HQFDDARLRS LLVKVLSQKN SIDDFEIKLK LPKVGERNLL
MNARQIKNER TQEQLILLAI EDKTEEAAAQ KIIDDNKKRA EKERKLLHDF FTQAPAVLAI
LKGPEHVFEF ANAAYMELVG QRDLKNKSVL EALPETESQG FIELLDKVYK TGETYIGKEL
SLKLDKKNEE SQLLYMNFVY QAFKNNNGDT EGILVYAHDV TEQVMSRKQI EASEKRFSNI
LEQSIMAIGI LKGTDMVISF ANAPLLDTWG KGDDVFGKPF FEVLPEIKDQ GFPELLQQVY
TTGVPHYGHE TKVTHFRWEK EETRYYNFVY QPYTEVDNSI TGITILATDV TDQVLAKKQI
EESENEQLML ARLLKLATDS AAVGIWSLDV VSSKLKWSNL HKKLWGYDEH REDLTYEDWH
NLIVPEDKKM ALQKIEEFKV NHGIYEVDYR IKRANDGAVI WIRSTGQYHY DDIGEAHTLS
GISLDITEHK SFTEELEIKV KERTAELKKS NEALKKTNTQ LDQFAHIASH DLQEPLRKIL
TFSMRLQDNH KAELSNEVQS YLDKIEGASS RMSTLIRDLL NYSRLLEHEK LVEKTNLNDT
LKNILNDFEL LVDEKKAEIK SDELPTIEAI PLQMNQLFYN LISNALKFSR EEVPPVITIT
SRTLSEKQIK KYPILNPLRS YVEIIFKDNG IGFEQQYSEK IFTIFQRLHN RDTFIGTGIG
LALTKKITEN HNGLTFADGQ ENVGASFHVI LPFEQPR
//
