ID   MTGA_HAEIE              Reviewed;         240 AA.
AC   A5UDP3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   13-SEP-2023, entry version 93.
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};
GN   OrderedLocusNames=CGSHiEE_07905;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UDP3; -.
DR   SMR; A5UDP3; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; hip:CGSHiEE_07905; -.
DR   HOGENOM; CLU_006354_1_1_6; -.
DR   UniPathway; UPA00219; -.
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; Biosynthetic peptidoglycan transglycosylase-like; 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   NCBIfam; TIGR02070; mono_pep_trsgly; 1.
DR   PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..240
FT                   /note="Biosynthetic peptidoglycan transglycosylase"
FT                   /id="PRO_1000017306"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ   SEQUENCE   240 AA;  28006 MW;  28B20DA4D6A6A2B8 CRC64;
     MKKTKRIFTA LSHLFSPKWW KKNWQRVVLL FFFAVFALLL IFRFVPIPFS AYMVQQKIAN
     LLQGDFRYQI QYDWVSLENI SPNIQLAVIS SEDQRFPEHL GFDFEAIQRA IRYNEKSNKG
     IRGASTISQQ TAKNLMLWHG QNWLRKGLEV PATMLLELTW SKKRILEVYL NIAEFGNGIF
     GVEAASRYYF KKSAKNLSQN EAALLVAVLP NPIIYKVNKP SLLVRKKTSL DFETNGKFRY
//