ID   CCRM_BRUA2              Reviewed;         377 AA.
AC   Q2YMK2; O30570; Q57EN0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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 BabI;
DE   AltName: Full=Orphan methyltransferase M.BabI {ECO:0000303|PubMed:12654995};
DE            Short=M.BabI {ECO:0000303|PubMed:12654995};
GN   Name=ccrM {ECO:0000303|PubMed:9294447}; Synonyms=babI, babIM;
GN   OrderedLocusNames=BAB1_0516;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2308;
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=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [3]
RP   FUNCTION, IMPORTANCE IN VIABILITY, INDUCTION, TRANSCRIPTIONAL CONTROL BY
RP   CTRA, AND DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=10852881; DOI=10.1128/jb.182.12.3482-3489.2000;
RA   Robertson G.T., Reisenauer A., Wright R., Jensen R.B., Jensen A.,
RA   Shapiro L., Roop R.M. II;
RT   "The Brucella abortus CcrM DNA methyltransferase is essential for
RT   viability, and its overexpression attenuates intracellular replication in
RT   murine macrophages.";
RL   J. Bacteriol. 182:3482-3489(2000).
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 on A-2 on both strands
CC       (PubMed:12654995) (By similarity). Overexpression from a moderate-copy
CC       number plasmid (10-12 copies/cell) leads to enlarged, branched cells,
CC       many with 3-5 genome equivalents. Contributes to the accurate cell-
CC       cycle control of DNA replication and cellular morphology
CC       (PubMed:10852881). {ECO:0000250|UniProtKB:O30569,
CC       ECO:0000269|PubMed:10852881, ECO:0000303|PubMed:12654995}.
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   -!- INDUCTION: By CtrA. {ECO:0000269|PubMed:9294447}.
CC   -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted.
CC       {ECO:0000269|PubMed:10852881}.
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; AF011895; AAB71351.1; -; Genomic_DNA.
DR   EMBL; AM040264; CAJ10472.1; -; Genomic_DNA.
DR   RefSeq; WP_002969465.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YMK2; -.
DR   SMR; Q2YMK2; -.
DR   STRING; 359391.BAB1_0516; -.
DR   REBASE; 11592; M.BmeAORF516P.
DR   REBASE; 3263; M.BabI.
DR   EnsemblBacteria; CAJ10472; CAJ10472; BAB1_0516.
DR   GeneID; 3788634; -.
DR   KEGG; bmf:BAB1_0516; -.
DR   PATRIC; fig|359391.11.peg.2554; -.
DR   HOGENOM; CLU_024927_5_1_5; -.
DR   OMA; WRKANPM; -.
DR   Proteomes; UP000002719; Chromosome I.
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   2: Evidence at transcript level;
KW   DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..377
FT                   /note="DNA methyltransferase CcrM"
FT                   /id="PRO_0000087986"
FT   DOMAIN          271..373
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  42202 MW;  657C88A25580B39D CRC64;
     MSLVRLAHEL PIEAPRTAWL DSIIKGDCVS ALERLPDHSV DVIFADPPYN LQLGGDLHRP
     DQSMVSAVDD HWDQFESFQA YDAFTRAWLL ACRRVLKPNG TIWVIGSYHN IFRVGTQLQD
     LGFWLLNDIV WRKTNPMPNF RGRRFQNAHE TLIWASREQK GKGYTFNYEA MKAANDDVQM
     RSDWLFPICT GSERLKDENG DKVHPTQKPE ALLARIMMAS SKPGDVILDP FFGSGTTGAV
     AKRLGRHFVG IEREQPYIDA ATARINAVEP LGKAELTVMT GKRAEPRVAF TSVMEAGLLR
     PGTVLCDERR RFAAIVRADG TLTANGEAGS IHRIGARVQG FDACNGWTFW HFEENGVLKP
     IDALRKIIRE QMAAAGA