CCRM_RHIME
ID CCRM_RHIME Reviewed; 376 AA.
AC O30569;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA methyltransferase CcrM {ECO:0000303|PubMed:9294447};
DE Short=M.CcrM;
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase SmeI;
DE AltName: Full=Modification methylase SmeI;
DE AltName: Full=Orphan methyltransferase M.SmeI {ECO:0000303|PubMed:12654995};
DE Short=M.SmeI;
GN Name=smeIM; Synonyms=ccrM {ECO:0000303|PubMed:9294447};
GN OrderedLocusNames=R00926; ORFNames=SMc00021;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=1021;
RX PubMed=9294447; DOI=10.1128/jb.179.18.5869-5877.1997;
RA Wright R., Stephens C., Shapiro L.;
RT "The CcrM DNA methyltransferase is widespread in the alpha subdivision of
RT proteobacteria, and its essential functions are conserved in Rhizobium
RT meliloti and Caulobacter crescentus.";
RL J. Bacteriol. 179:5869-5877(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
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 [4]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: A beta subtype methylase that recognizes the double-stranded
CC sequence 5'-GANTC-3' and methylates A-2 on both strands (Probable)
CC (PubMed:12654995). Overexpression leads to many branched and bloated
CC cells, two to three times the size of wild-type cells, and cells that
CC have 1-3 times the normal amount of DNA. Contributes to the accurate
CC cell-cycle control of DNA replication and cellular morphology. Can
CC fully replace its ortholog in C.crescentus (PubMed:9294447).
CC {ECO:0000269|PubMed:9294447, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:9294447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted.
CC {ECO:0000269|PubMed:9294447}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF011894; AAB71350.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45498.1; -; Genomic_DNA.
DR RefSeq; NP_385032.1; NC_003047.1.
DR RefSeq; WP_010968922.1; NC_003047.1.
DR AlphaFoldDB; O30569; -.
DR SMR; O30569; -.
DR STRING; 266834.SMc00021; -.
DR REBASE; 101147; M.Rga602ORF1036P.
DR REBASE; 101328; M.Ret4803ORF999P.
DR REBASE; 152633; M.Rsp6212ORF1017P.
DR REBASE; 152636; M.Rsp621ORF1018P.
DR REBASE; 152639; M.Ret561ORF1010P.
DR REBASE; 152648; M.Rsp1341ORF1010P.
DR REBASE; 152651; M.Rsp1314ORF1036P.
DR REBASE; 152656; M.Rsp113ORF1012P.
DR REBASE; 152663; M.Rph744ORF1023P.
DR REBASE; 152667; M.Rph723ORF1024P.
DR REBASE; 152670; M.Rph650ORF1058P.
DR REBASE; 152675; M.Rph630ORF1029P.
DR REBASE; 152677; M.Rph620ORF1038P.
DR REBASE; 152683; M.Rph611ORF1058P.
DR REBASE; 152693; M.Rph931ORF1019P.
DR REBASE; 152698; M.Rph841ORF1047P.
DR REBASE; 152719; M.Rph831ORF1016P.
DR REBASE; 152721; M.Rph771ORF1021P.
DR REBASE; 152726; M.Rph671ORF1021P.
DR REBASE; 152730; M.Rph261ORF1022P.
DR REBASE; 152742; M.Rph161ORF1027P.
DR REBASE; 152743; M.Rsp871ORF1010P.
DR REBASE; 152744; M.Rsp741ORF1010P.
DR REBASE; 152747; M.Rsp731ORF1036P.
DR REBASE; 152757; M.Rsp324ORF1085P.
DR REBASE; 152765; M.Rsp541ORF1046P.
DR REBASE; 152773; M.Rsp941ORF1046P.
DR REBASE; 175266; M.Rga4872ORF1074P.
DR REBASE; 175279; M.Ret8C3ORF1033P.
DR REBASE; 201007; M.RspNXC14ORF1043P.
DR REBASE; 201810; M.RetNXC12ORF1021P.
DR REBASE; 211750; M.RphB5ORF1036P.
DR REBASE; 211751; M.RspK5ORF1114P.
DR REBASE; 211754; M.Rsp894ORF993P.
DR REBASE; 211755; M.RspL182ORF1031P.
DR REBASE; 232572; M.RspNXC24ORF960P.
DR REBASE; 233040; M.SfrNXT3ORF945P.
DR REBASE; 3264; M.SmeI.
DR REBASE; 68117; M.RetMim1ORF1016P.
DR REBASE; 87689; M.Ret4771ORF1041P.
DR EnsemblBacteria; CAC45498; CAC45498; SMc00021.
DR GeneID; 61602391; -.
DR KEGG; sme:SMc00021; -.
DR PATRIC; fig|266834.11.peg.2324; -.
DR eggNOG; COG2189; Bacteria.
DR HOGENOM; CLU_024927_5_1_5; -.
DR OMA; WRKANPM; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR040843; RAMA.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18755; RAMA; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..376
FT /note="DNA methyltransferase CcrM"
FT /id="PRO_0000087988"
FT DOMAIN 273..370
FT /note="RAMA"
FT /evidence="ECO:0000255"
FT CONFLICT 135..141
FT /note="NPMPNFK -> QPDAELQ (in Ref. 1; AAB71350)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="P -> A (in Ref. 1; AAB71350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41442 MW; 790DE7FE3D22900A CRC64;
MSSVVSLAEI SRAARPLNWL DSIIKGDCVA ALNALPDHSV DVVFADPPYN LQLGGTLHRP
DQSLVDAVDD DWDQFASFEA YDAFTRAWLL ACRRVLKPTG TLWVIGSYHN IFRVGAILQD
LHFWVLNDII WRKTNPMPNF KGRRFQNAHE TLIWATPNAK AKGYTFNYEA MKAANDDVQM
RSDWLFPICS GSERLKGDDG KKVHPTQKPE ALLARILMAS TKPGDVVLDP FFGSGTTGAV
AKRLGRHFVG IEREQDYIDA AAERIAAVEP LGKATLSVMT GKKAEPRVAF NTLVESGLIK
PGTVLTDAKR RYSAIVRADG TLASGGEAGS IHRLGAKVQG LDACNGWTFW HFEEGSVLKP
IDELRSVIRN DLAKLN
