ID A0A0G1BB39_9BACT Unreviewed; 1063 AA.
AC A0A0G1BB39;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN ORFNames=UV05_C0030G0007 {ECO:0000313|EMBL:KKS43566.1};
OS candidate division CPR1 bacterium GW2011_GWA2_42_17.
OC Bacteria; candidate division CPR1.
OX NCBI_TaxID=1618341 {ECO:0000313|EMBL:KKS43566.1, ECO:0000313|Proteomes:UP000034875};
RN [1] {ECO:0000313|EMBL:KKS43566.1, ECO:0000313|Proteomes:UP000034875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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:KKS43566.1}.
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DR EMBL; LCCZ01000030; KKS43566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1BB39; -.
DR PATRIC; fig|1618341.3.peg.504; -.
DR Proteomes; UP000034875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..249
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 286..597
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 805..1032
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
SQ SEQUENCE 1063 AA; 119327 MW; 516364867A72C758 CRC64;
MLIKSGLGRK YRFPGHRREV EETAPWSVPG VENKRASISG WHIWLWLAGV VVLVAFGFRL
FWLQAVQQKY WTELASKNQF SEKPILAPRG EIVTRDGKVI ATSQSRVSMW FDPKVAGTDG
FTVAREEIFK LLSFWSDGKK LWPALPPEKI SPVLENLPQQ VASVILAQTA LPAGLLVKEE
MTRFYPFDDI FSHVVGYVGP PSKAQQKGGE ILPYEKVGQS GLEASYEESL HGERGTEFIQ
ADAAGRYFEV RNIYFPKPGD KFNATLHYGL QNEIAIAMKN ISKPAVAVML DANTGEIYAL
YNKPSFSPNG LIAGDNKKII EALDPKKQPL LNRAVLGQYP SGSLFKIVTA LAGLAEHIIT
PQATVLSTGG IKLGDHFFPD WKAGGHGITN LAKALAESVN TFFYAVGGGG LGYDGMGASR
LAEYARAFGL AQKTGVDLPN EAVGALPDPV KRKKLTGESW YQGDTYNFAI GQGDVLVTPL
QIARAYSVVV SGGRLVQPHL NRDLIMTYKM IDYSEYLPTI LVGLKQNITA GSGRELQSVS
LNLYGKTGTA QYAKNKTHAW FVSFIKDEKG LPPLVLVVLV EGGGEGSSVA LPVARDVWTW
VKQINKEMID NLKSDTNALL SFLQNQNDGI IIYTLGKLGR LENGYSREPL VSLLNNKNDD
IRVLSIKNLA KIGDISLLPT FIQYAHSDES TEVRRESVSA IGRLRDEKTV PILVEFLKDN
DPKVVMQAIR GLLVFSEKED VRNALKKLID HPNELIQEVI NKELNGSLYK LDNSQNQVDF
PNQLRNAIIH GDAKNALKHM PDESIHLTFT SPPYYNARDY SIYQSYDEYL KFLESIFKEV
HRITKAGRFF ILNTSPIIIP RISRAHSSKR YPIPYDIHPL LIKMGWEFID DIVWVKSEAS
VKNRNAGFLQ HRKPLAYKPN AVTEMIMVYR KKFDRLIDWN IQQYSWDTVK KSKVLDKYET
SNVWRIEPTF DKVHSAVFPI ELCNRVIRLY SFVGDLVFDP FAGSGTVGRA AINLERNFCL
VEKEAKYVSR IKEEFNNNMN LFACDNNYPK YFDLENFIKS SNI
//
