MTGA_CYTH3
ID MTGA_CYTH3 Reviewed; 244 AA.
AC Q11VI0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=CHU_1314;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(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; CP000383; ABG58586.1; -; Genomic_DNA.
DR RefSeq; WP_011584701.1; NZ_FPJX01000009.1.
DR AlphaFoldDB; Q11VI0; -.
DR SMR; Q11VI0; -.
DR STRING; 269798.CHU_1314; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; ABG58586; ABG58586; CHU_1314.
DR KEGG; chu:CHU_1314; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_1_10; -.
DR OMA; PAPKCFD; -.
DR OrthoDB; 1793788at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001822; 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..244
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000257666"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ SEQUENCE 244 AA; 28231 MW; 2E6D853D5609586F CRC64;
MYIEIIFSCK QLMKKAKIIL LTCCIYFFVY TFQIVLVFKF VNPVVTPLMI VRVAEGVFSK
EYVGIRKTWK PIKEISPNMV CAVIASEDHH FLEHNGFDWE AIRAARAYNE RHKNGIKRGA
STISQQTAKN VFLFPSRSWI RKGFEAYFTF LIELLWSKER IMEMYLNEIE MGKGIYGIEA
AAQKYYHIPA KKLSQQQAAS IAAILPLPLK RNPLKPGKNT ASRVLWIRSQ MSSVEKPTWI
LKSK
