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MTGA_SHEDO
ID   MTGA_SHEDO              Reviewed;         229 AA.
AC   Q12Q34;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=Sden_1156;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000302; ABE54442.1; -; Genomic_DNA.
DR   RefSeq; WP_011495603.1; NC_007954.1.
DR   AlphaFoldDB; Q12Q34; -.
DR   SMR; Q12Q34; -.
DR   STRING; 318161.Sden_1156; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   EnsemblBacteria; ABE54442; ABE54442; Sden_1156.
DR   KEGG; sdn:Sden_1156; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_1_1_6; -.
DR   OMA; PAPKCFD; -.
DR   OrthoDB; 1793788at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001982; 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..229
FT                   /note="Biosynthetic peptidoglycan transglycosylase"
FT                   /id="PRO_1000017316"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ   SEQUENCE   229 AA;  26025 MW;  39DF2560F020F119 CRC64;
     MTVRRRGFMA WTWFITWRFL LVVVLLLLVL LLVLRFVPPP TTSFMLQSAY PVSQHWVSID
     ELPSHLPLAV VASEDQLFPK HFGIDFTSIT KALNQYDDGQ GLRGASTITQ QTAKNLLLWP
     GRNLVRKGLE AMLAVSLEAV WGKKRILEVY LNVAEFGKGI YGVEAASRHY FNKSARYLSI
     NEAARLAVLL PSPRSRSPHH LTPYLHQRVA WGEKQMRQLG SGYLKTILN
 
 
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