MTGA_ACIAD
ID MTGA_ACIAD Reviewed; 224 AA.
AC O24849;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00766};
DE AltName: Full=Glycan polymerase {ECO:0000255|HAMAP-Rule:MF_00766};
DE AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000255|HAMAP-Rule:MF_00766};
DE Short=PGT {ECO:0000255|HAMAP-Rule:MF_00766};
GN Name=mtgA {ECO:0000255|HAMAP-Rule:MF_00766}; OrderedLocusNames=ACIAD1061;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7670642; DOI=10.1099/13500872-141-6-1425;
RA Geissdoerfer W., Frosch C.S., Haspel G., Ehrt S., Hillen W.;
RT "Two genes encoding proteins with similarities to rubredoxin and rubredoxin
RT reductase are required for conversion of dodecane to lauric acid in
RT Acinetobacter calcoaceticus ADP1.";
RL Microbiology 141:1425-1432(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9074511; DOI=10.1016/s0378-1119(96)00728-7;
RA Geissdoerfer W., Ratajczak A., Hillen W.;
RT "Nucleotide sequence of a putative periplasmic Mn superoxide dismutase from
RT Acinetobacter calcoaceticus ADP1.";
RL Gene 186:305-308(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC elongation from lipid-linked precursors. {ECO:0000255|HAMAP-
CC Rule:MF_00766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00766};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00766}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00766}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00766}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000255|HAMAP-Rule:MF_00766}.
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DR EMBL; Z46863; CAA86932.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG67949.1; -; Genomic_DNA.
DR RefSeq; WP_004921655.1; NC_005966.1.
DR AlphaFoldDB; O24849; -.
DR SMR; O24849; -.
DR STRING; 62977.ACIAD1061; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR DNASU; 2879151; -.
DR EnsemblBacteria; CAG67949; CAG67949; ACIAD1061.
DR GeneID; 45233503; -.
DR KEGG; aci:ACIAD1061; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_1_6; -.
DR OMA; PAPKCFD; -.
DR OrthoDB; 1793788at2; -.
DR BioCyc; ASP62977:ACIAD_RS04890-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; -; 1.
DR HAMAP; MF_00766; PGT_MtgA; 1.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR011812; Pep_trsgly.
DR PANTHER; PTHR30400; PTHR30400; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR TIGRFAMs; TIGR02070; mono_pep_trsgly; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..224
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000083114"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ SEQUENCE 224 AA; 26713 MW; F1E5F114FC14E2FE CRC64;
MKRFIVRAVL ILVSFVLLIQ LWIFCSLAWW RTHPVETTMF MRLDYWSDSS KPIQQQWRDY
DEISDNFKKA VVAAEDGKFV HHHGFDWEGI QYALEKNEKS GEVVNGGSTI SQQLAKNLFL
YNQRSLIRKG QEAIATWMME RMWSKQRILE VYMNSVQFGD HLYGVEAASH YYFHRSAQNL
TRDQAAFLAA LLPNPKYYQE NRNDPRFKFK KRFTLKYMRY SEIP
