ID A0A239PQB7_9PROT Unreviewed; 691 AA.
AC A0A239PQB7;
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=SAMN06297382_1280 {ECO:0000313|EMBL:SNT72243.1};
OS Amphiplicatus metriothermophilus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Parvularculales; Parvularculaceae; Amphiplicatus.
OX NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT72243.1, ECO:0000313|Proteomes:UP000198346};
RN [1] {ECO:0000313|EMBL:SNT72243.1, ECO:0000313|Proteomes:UP000198346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT72243.1,
RC ECO:0000313|Proteomes:UP000198346};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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; FZQA01000002; SNT72243.1; -; Genomic_DNA.
DR RefSeq; WP_234993319.1; NZ_FZQA01000002.1.
DR AlphaFoldDB; A0A239PQB7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198346; 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:UP000198346};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 65..231
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 306..569
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 601..685
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 691 AA; 73002 MW; 23AE4C1831D44C87 CRC64;
MKTARRLFRS HFAPVMRIAA AALALLGAVA AADLLFPPPL HKGEALSPLV LDREGRWLQA
FTTADGRWRF RADLDAVDPS FVERLIAVED KRFHAHWGVD PIALARASGE ALRAGRIASG
ASTITMQTAR LLEPRPRTVG AKLVEVIRAL QIERRLTKRE ILELYLTLAP YGGNIEGVRA
ASLLYFGKEP AHLTDAEQAL LIALPQAPEA RRPDRRPDSA RAARAAILEK LAAQGLLSPA
RAEEARLASL PETRRPFPRA AWHAAAALAK EGAPVVRSTI DLVLQREAEA LVAAWAAGLD
DGATAAALIV ETETRAVRAA VGSSGLDAPG GWIDLTAAVR SPGSTLKPFI YALAFDDGLI
GPHTVIEDMP QSFDGYAPEN FDRRFHGEVR AGEALKHSLN LPAVRLLDRL GANRLAAVLR
AAGAALAAPE SAEGDFGLAL ALGGAGVTMR DLAALYAGLA DEGRARPLAW KAEEAEAPAA
PAYRLFSAQS AARVSAVLAD APALEGRAPA ALTVRAPKIA MKTGTSYGYR DAWAAGHAGG
YTVVVWVGRA DGAPRPGATG RKAAAPLLAA LFDMIWRADP AAARAVPEIG ESESPALARL
AAPRRERAPE IVFPRDGAEL FAATDEARGF SLAARGGAGG YRWYVSGEPA ATEPTSGRAL
WRPRAAGFYE IVVVDGAGRS ARAKVRVLTE G
//
