ID A0A1H3EAD3_ALLWA Unreviewed; 691 AA.
AC A0A1H3EAD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN05421644_11217 {ECO:0000313|EMBL:SDX75651.1};
OS Allochromatium warmingii (Chromatium warmingii).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Chromatiales; Chromatiaceae; Allochromatium.
OX NCBI_TaxID=61595 {ECO:0000313|EMBL:SDX75651.1, ECO:0000313|Proteomes:UP000198672};
RN [1] {ECO:0000313|Proteomes:UP000198672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 173 {ECO:0000313|Proteomes:UP000198672};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; FNOW01000012; SDX75651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3EAD3; -.
DR STRING; 61595.SAMN05421644_11217; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198672; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198672};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 56..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 308..537
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 600..688
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 691 AA; 74707 MW; C8397BB932E11F5B CRC64;
MTTAAPLKPR IFFPLLACIL SASFWLGFEH WINTAPLPDL RVATSAQCLD RNGRLLRAFP
VTDGRWRLPI TPDAVDPRYL TRLLAIEDQR FYQHSGVDPL ALLRAAWQWL RDGRIVSGGS
TLTMQVARRL DGRSTRTLGG KLQQIRLALA LERQLDKNAI LTAYLHLIPQ GGNLEGVRSG
ALAWLGHEPQ RLTAAESALL IALPQAPETR RPDRNPQALH RARDAILQRL HAADLIDALE
LTAARREPLP HQRRPLPLLA AHLTARQQHA HPERASQHLT LDAQLQQRLE ILAADRAAAL
GERVSLALLV AEHTTGEIWA AVGSPALLDE ARRGHLDMTR AIRSPGSTLK PLIYGLAFED
GIAHPESLIE DRPSGFDGYA PSNFDRAFQG TVSVRHALHA SLNIPAVRLL HAVGPARLMA
RLRRAGVQPV LPHGSAPGLA IGLGGIGVHL TDLVQLYAAL ARGGAPIAVR ATREPATADP
LMRPVLDARA AWLVSSVLAG VPAPDRANAA QIAFKTGTSY GYRDAWALGF DGRWVVGVWT
GRADGAPVPG LAGIDAAAPV LIDVFAQLGP RTPLPPPPPG VRPLRHAELP EMLRHVPAAH
RTADATDTLE IAYPPANARI DLGLTRGGSA TALVLRVRGG TPPFTWFADS EPIAREPFSR
NTHWTPKGSG YMTLVVVDGR GASARVRVRV E
//
