ID A0A178MKI0_9PROT Unreviewed; 1510 AA.
AC A0A178MKI0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=A6A04_20090 {ECO:0000313|EMBL:OAN48555.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN48555.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN48555.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN48555.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) 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:OAN48555.1}.
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DR EMBL; LWQT01000074; OAN48555.1; -; Genomic_DNA.
DR RefSeq; WP_068493991.1; NZ_LWQT01000074.1.
DR STRING; 1285242.A6A04_20090; -.
DR OrthoDB; 5287260at2; -.
DR Proteomes; UP000078428; 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:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR44757:SF2; BIOFILM ARCHITECTURE MAINTENANCE PROTEIN MBAA; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000078428};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..194
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 208..470
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 828..895
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 949..995
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1022..1074
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1106..1238
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 1247..1501
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT COILED 635..697
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 17
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1510 AA; 168524 MW; 4955A7BCA93FCA5F CRC64;
MDVKVDNKPH VIGIGASAGG LEALSQFVAG LPLDLGCIYV VAQHMSPTHR SMMADILSRE
TRLPVRELAD GERPQPDVIY IIPPGTNLVF KDECFVLSQA SPEISPKPSI NILFQSMADE
FEERAIGIIL SGTGSDGTRG LRAIKSAGGI TFVQIPESAK YDGMPRSAID ACVADRIVSP
DQIGRELERL VRFPGMLPNL ESGEQRPAEL SDLFERVRLR TKIDFSSYKL STVQRRLQRR
MAATNTGTLA EYLSKTDTDP DELDALAKET LISVTEFFRD KDAFRALERH TREIVGRKLP
GEEIRVWVVG CATGEEAYSL AIMFSELISE RGIGSRLQVF ATDIDNNAMS VARRGIYNQT
AMAEMPQEYV SKYFIPCGNG FEPTKELRDC VTFARQDVNV DPPFLRLDLV TCRNVMIYFN
SDLQAKVLSI LRYSLREDGL LFLGRSETVT QQEAMFASVD RRARIFRPRG QSRPITMGKL
VRGQLKVPKY EPRNPDRSNE RIFLNALADQ FGPAMLIDSG CRILHSHGPV SRFIHFPTGT
PEMNLAQLIV PEFSNEILTT MHRARRRQAS SYSRKRRIAS LDKQVWRLAV HPVGQQAEAD
TFLVVFERSA QSDAANAVRE AESQDGSEVF PDDELASTRE HLQTLMEEMA ASNEEMQALN
EEVQAANEEL QASNEELEAS NEELQATNEE LVSVNEESLI KSAELSAINS DFEGVYNTID
FPIMVFDPEL FLKRANGAAV KTYDLPLSAS GMHIGRLKLP AFLDNIDKSL TAALTEQRKE
SFQITFGKRT FQVFVTPSMS LTGTPLSVVL VVVDHTDLVE AQEQIRESQE RLLSIMNHST
SAVSLKDAAG RYEFINMRFE ELFGITAEQV IGKTDQQLFS RDIAQLLRSR DLEVMGQLSA
IQHLEEMVFP TSKVWLDSVR FPIFDSNGVV RAVCSQSTDV TMKHHAEEQL RLAAKVFDRA
GEAITITDSS GNIITVNDSF FRITGYSHQE VIGKNPRFLQ SGKHGKDFYD AMWRSLIEQG
CWQGEIFNRR KNGEIYPEWL TVNSVRDENG SVVNYVAIFS DISAIKSSQR RIEFLATHDE
LTGIPNRSLL MDRLKHAVAQ AKRQKTKLAV LFIDLDNFKV INDSLGHDVG DQLLKQATER
LKHCVRDSDT LARLGGDEFV AVLTDVSLEK VNSVASRIVD FLGASFSIND KSLFVSASMG
ISVFPDDGED SLTLLKHADT AMYRAKERGR NQYQFFADEM KVIALQRLTL ETGLRLALET
NSFRMCYQPQ VDIHTGEVVG AEALLRWRDP NLGEVSPAHF IPIAESCGLI GAIGETVFTM
VLEQIAYWRD KGLTVPRIAI NVSAHQLRDA GFAAKVGSWL DNSGISSELI GIELTESALM
ERIDMVKEML TSFDGMGMKV SIDDFGTGYS SLSYLKKLPI HELKIDRSFV DGIALERDDR
SIAKAIIDMS RALGMRVVAE GVESEDQLGV LKEEGCDMVQ GYLFHRPLSP EAFAKVIESG
GKSSRKPPKR
//
