ID   CCRM_CAUVN              Reviewed;         358 AA.
AC   B8GZ33; Q45971;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=DNA methyltransferase CcrM {ECO:0000303|PubMed:8577742};
DE            Short=M.CcrMI {ECO:0000303|PubMed:9294447};
DE            EC=2.1.1.72 {ECO:0000305|PubMed:8289276};
DE   AltName: Full=Adenine-specific methyltransferase CcrMI;
DE   AltName: Full=Type II methyltransferase M.CcrNAI {ECO:0000303|PubMed:12654995};
DE            Short=M.CcrNAI {ECO:0000303|PubMed:12654995};
GN   Name=ccrMIM; Synonyms=ccrM {ECO:0000303|PubMed:8289276};
GN   OrderedLocusNames=CCNA_00382;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=8289276; DOI=10.1006/jmbi.1994.1007;
RA   Zweiger G., Marczynski G., Shapiro L.;
RT   "A Caulobacter DNA methyltransferase that functions only in the
RT   predivisional cell.";
RL   J. Mol. Biol. 235:472-485(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=8577742; DOI=10.1073/pnas.93.3.1210;
RA   Stephens C., Reisenauer A., Wright R., Shapiro L.;
RT   "A cell cycle-regulated bacterial DNA methyltransferase is essential for
RT   viability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1210-1214(1996).
RN   [4]
RP   PROTEOLYTIC DEGRADATION.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=8666236; DOI=10.1101/gad.10.12.1532;
RA   Wright R.J., Stephens C., Zweiger G., Shapiro L., Alley M.K.R.;
RT   "Caulobacter Lon protease has a critical role in cell-cycle control of DNA
RT   methylation.";
RL   Genes Dev. 10:1532-1542(1996).
RN   [5]
RP   FUNCTION.
RC   STRAIN=NA1000 / CB15N;
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   [6]
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 non-modifed A-2 on the
CC       hemimethylated, post-replicative DNA (PubMed:12654995) (Probable).
CC       Functions only in the predivisional cell. Responsible for 5'-GANTC-3'
CC       methylation in the cell; remethylation of hemimethylated sites
CC       generated after replication fork passage occurs late in the
CC       predivisional cell, near completion of chromosome replication but prior
CC       to cell division. Constitutive expression of the methylase leads to
CC       morphologically aberrant cells as well as cells that have undergone
CC       additional chromosome replication. Contributes to the accurate cell-
CC       cycle control of DNA replication and cellular morphology
CC       (PubMed:8289276, PubMed:8577742). Opens a bubble in the DNA at the
CC       recognition site, allowing precise recognition of the sequence and
CC       ensuring enzyme specificity (By similarity). Can fully replace its
CC       ortholog in R.meliloti (PubMed:9294447). {ECO:0000250|UniProtKB:P0CAW2,
CC       ECO:0000269|PubMed:8289276, ECO:0000269|PubMed:8577742,
CC       ECO:0000269|PubMed:9294447, ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:8289276}.
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         Evidence={ECO:0000305|PubMed:8289276, ECO:0000305|PubMed:8577742};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0CAW2}.
CC   -!- DEVELOPMENTAL STAGE: In synchonized cells transcribed (PubMed:8289276)
CC       and protein expressed (PubMed:8577742) only in predivisional cells
CC       (from 80 minutes) with a peak at 120 minutes, protein levels drop
CC       precipitously prior to cell division (at protein level).
CC       {ECO:0000269|PubMed:8289276, ECO:0000269|PubMed:8577742}.
CC   -!- INDUCTION: Transcribed from 80 minutes in synchronized cells.
CC       {ECO:0000269|PubMed:8289276}.
CC   -!- DOMAIN: Has an N-terminal methyltransferase (MTase) domain linked to a
CC       C-terminal DNA-binding domain by a 10 residue linker. The MTase of one
CC       monomer recognizes, binds and modifies the target strand while C-
CC       terminal domain of the other monomer binds the non-target strand.
CC       {ECO:0000250|UniProtKB:P0CAW2}.
CC   -!- PTM: Rapidly degraded by Lon protease prior to cell division.
CC       {ECO:0000269|PubMed:8666236}.
CC   -!- DISRUPTION PHENOTYPE: Essential, it cannot be disrupted.
CC       {ECO:0000269|PubMed:8577742}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U01032; AAA18913.1; -; Unassigned_DNA.
DR   EMBL; CP001340; ACL93849.1; -; Genomic_DNA.
DR   PIR; S43876; S43876.
DR   RefSeq; WP_010918266.1; NC_011916.1.
DR   RefSeq; YP_002515757.1; NC_011916.1.
DR   AlphaFoldDB; B8GZ33; -.
DR   SMR; B8GZ33; -.
DR   REBASE; 19987; M.CcrNAI.
DR   GeneID; 7331081; -.
DR   KEGG; ccs:CCNA_00382; -.
DR   PATRIC; fig|565050.3.peg.381; -.
DR   HOGENOM; CLU_024927_5_1_5; -.
DR   OrthoDB; 9800801at2; -.
DR   PhylomeDB; B8GZ33; -.
DR   Proteomes; UP000001364; 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   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..358
FT                   /note="DNA methyltransferase CcrM"
FT                   /id="PRO_0000378305"
FT   DOMAIN          259..355
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
FT   REGION          1..260
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P0CAW2"
FT   REGION          261..270
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:P0CAW2"
FT   REGION          272..358
FT                   /note="Non-specific DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0CAW2"
FT   CONFLICT        242
FT                   /note="Y -> D (in Ref. 1; AAA18913)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  39665 MW;  05F43266F7D4C614 CRC64;
     MKFGPETIIH GDCIEQMNAL PEKSVDLIFA DPPYNLQLGG DLLRPDNSKV DAVDDHWDQF
     ESFAAYDKFT REWLKAARRV LKDDGAIWVI GSYHNIFRVG VAVQDLGFWI LNDIVWRKSN
     PMPNFKGTRF ANAHETLIWA SKSQNAKRYT FNYDALKMAN DEVQMRSDWT IPLCTGEERI
     KGADGQKAHP TQKPEALLYR VILSTTKPGD VILDPFFGVG TTGAAAKRLG RKFIGIEREA
     EYLEHAKARI AKVVPIAPED LDVMGSKRAE PRVPFGTIVE AGLLSPGDTL YCSKGTHVAK
     VRPDGSITVG DLSGSIHKIG ALVQSAPACN GWTYWHFKTD AGLAPIDVLR AQVRAGMN
//