ID A0A2T6FGE3_9GAMM Unreviewed; 799 AA.
AC A0A2T6FGE3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=B0W54_13295 {ECO:0000313|EMBL:PUA27535.1};
OS Cellvibrio sp. 79.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Cellvibrionales; Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA27535.1, ECO:0000313|Proteomes:UP000243979};
RN [1] {ECO:0000313|EMBL:PUA27535.1, ECO:0000313|Proteomes:UP000243979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79 {ECO:0000313|EMBL:PUA27535.1};
RA Zhang Y., Xu J., Wang N.;
RT "Cellvibrio sp. 79 recovered from metagenome.";
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUA27535.1}.
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DR EMBL; MVDH01000003; PUA27535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FGE3; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000243979; 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 Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 62..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 317..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 703..789
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 799 AA; 90025 MW; 185B324FDC27A4AE CRC64;
MKLWRWSRVW ISRHKFLTSL LLLFCLSVGW LQFSSLPASL YSTPYASLLL ARDGSLLGAS
IAADQQWRFA PIEQLPDKYK NSLLLFEDRH FYRHPGINPL SIARALRGNI SAGKITSGGS
TLTMQLARLL RQETYRAEEK NSGRTLGNKI QEAALALKLE WRFSKEDLLI HYTSHAPYGG
NIVGLRAAAW RYFGRSPEYL SWSESALLAV LPNSPALIHP GRQRDVLLQK RNRLLQRLHA
QHYFSDLDLQ LALLEPLPER PQVLPQLAPH LLPTLKQKSP EQKVFNSTID PQLQQLANQI
ALRHSNRLVN DGVNNIALVL VDHQSMQTLA YVGNEAFQNK ISAAPSVDIV QRPRSTGSIL
KPLLYGLMLQ EGELAPTSLI ADIPTQINGY NPKNYDRSFR GAVPAQFALA HSLNIPAVRM
LRDYGIGRFQ EKLQAMGMTS LFRPADDYGL TLILGGAEGT LWELTGIYAR LAASARDGEI
NQSAMQVLIE KNNSGLLQVK PVFNQGSAWL TLQALIEVAR PGNDNYWRDF AGSQTIAWKT
GTSYGLRDAW AIGSNGRYTL GVWVGNAGGE PATFISGQSS AAPILFDMFD ALPKVNWFAK
PAHALKIISV CKDDGYLAGG QCEAMDMEIP RSSHFEKITP YHRIIHVDKD EQFRVHNRCE
TVSNMQSANW FLLPPTQEFY WRQHHSEYRT LPPWRRDCLA DSAQVDDDNP MELIYPQAHS
RIYIPVDLDG KRSRVVLKAV HRDAAATLYW HLDDEFLGET KVFHEREASL EPGVHKLLVM
DKNGYKLERR FNVIGEGNK
//
