ID   MTGA_BDEBA              Reviewed;         250 AA.
AC   Q3V7R3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Bd2847;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842653; CAE80628.1; -; Genomic_DNA.
DR   RefSeq; WP_011165231.1; NC_005363.1.
DR   AlphaFoldDB; Q3V7R3; -.
DR   SMR; Q3V7R3; -.
DR   STRING; 264462.Bd2847; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; CAE80628; CAE80628; Bd2847.
DR   KEGG; bba:Bd2847; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_1_1_7; -.
DR   OMA; PAPKCFD; -.
DR   OrthoDB; 1793788at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008080; 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..250
FT                   /note="Biosynthetic peptidoglycan transglycosylase"
FT                   /id="PRO_0000257657"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ   SEQUENCE   250 AA;  28927 MW;  5F358761E1D20006 CRC64;
     MRSRWQTLRK WIVKAVLLFF VSSLGFVLLY RFVPVPLTPL MVIRSVSSVW GEEFVGIHKD
     WVPLEEIAPS VQKAVLKAED YRFFEHNGFD FDAIEKAMKY NKTHKRKKGA STITQQTAKN
     VFLWPQRDWV RKGLEAYFTI LIESTWPKER IMEVYLNVIE LGPGVYGVEA ASQKYFKRSA
     KNLNPYQASL IAAVLPNPRR FRIDRPSNYV VGRQRRILNR VAPAIPKAAD ASLLDFLDLK
     FDSEEDESAN