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   27-MAR-2024, entry version 125.
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; Pseudomonadota; 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}.
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; 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   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   OrthoDB; 9800801at2; -.
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; Vaccinia Virus protein VP39; 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   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   Pfam; PF18755; RAMA; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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
//