ID A0A1I4F823_9GAMM Unreviewed; 733 AA.
AC A0A1I4F823;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN05192579_11625 {ECO:0000313|EMBL:SFL14054.1};
OS Rhodanobacter glycinis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Lysobacterales; Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=582702 {ECO:0000313|EMBL:SFL14054.1, ECO:0000313|Proteomes:UP000198725};
RN [1] {ECO:0000313|Proteomes:UP000198725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MO64 {ECO:0000313|Proteomes:UP000198725};
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; FOSR01000016; SFL14054.1; -; Genomic_DNA.
DR RefSeq; WP_092704950.1; NZ_FOSR01000016.1.
DR AlphaFoldDB; A0A1I4F823; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198725; 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:TreeGrafter.
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; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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:UP000198725};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 66..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 310..531
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 626..699
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 733 AA; 79209 MW; 3E2082D5FCB0D404 CRC64;
MRRWLTGVAA LAVVAAVVLA VATWRALPPL PAALVSASSS SVPLHVVAAD GTPLNRSYRG
RFNHVDALPA WRIPALLRTA FVASEDQRYW QHGGVDWRAR FAALWGNLRA GQVQRGASTI
GEQVARILQP RPHTYWSHWV AGIEAGRLLR RFGHAQVLDF YLNQVPYGAR RRGVAQAAHY
YFGRDPDALD PAEQLSLAVL VRSPSRYDPR RHPQALRQAV DQLAGRMRAS GAIDATQAEA
IRRAPIQPGQ QALAVEAGPF VLHAAERARA LGLTGPVLKT TLDPDLQRFV QQVLGQRVRT
LATRGVRNAA ALVVDNATGA VLAWVVAPQD GPFAIDAVLA PRQPGSTLKP FVYGLAMARL
GWQPDTVIED TPLAENVREG LHRYRNYSGR YYGKVSLRYA LANSLNIPAV KTAQAVGVPA
ILDLLHRLGF GTFEQTADFY GPAIVLGDGG VRLFDLVQGY ASLARHGRYL PLHVLADTPQ
PDPVPVLPAP VTSLLASILS DPNARSAEFG ADSVLDLPMP TAVKTGTSSD YRDIWTMGFD
DRYTVGVWMG RLDGGSTDGL TGSSGPAPVL RQIFARLRTA APYAGLWHSP ALQPVHTCEW
IGPPPCVQRD DWHLGDVHAP VSAPSTTTRR VAIARPLPGE MLAIDPRLPA ATQRYRFSLD
TAGQAIKRVV WQLDGKPLAT TTEAATSWQI VPGPHTLSVR VWLDGGNPGH ALELGPVAFS
VLGQAPPHEG SPE
//
