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Database: UniProt
Entry: A0A7W3YDW2_9GAMM
LinkDB: A0A7W3YDW2_9GAMM
Original site: A0A7W3YDW2_9GAMM 
ID   A0A7W3YDW2_9GAMM        Unreviewed;       795 AA.
AC   A0A7W3YDW2;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN   Name=pbpC {ECO:0000313|EMBL:MBB1087571.1};
GN   ORFNames=H4F99_03605 {ECO:0000313|EMBL:MBB1087571.1};
OS   Marilutibacter penaei.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Marilutibacter.
OX   NCBI_TaxID=2759900 {ECO:0000313|EMBL:MBB1087571.1, ECO:0000313|Proteomes:UP000552587};
RN   [1] {ECO:0000313|EMBL:MBB1087571.1, ECO:0000313|Proteomes:UP000552587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-8 {ECO:0000313|EMBL:MBB1087571.1,
RC   ECO:0000313|Proteomes:UP000552587};
RA   Xu S., Li A.;
RL   Submitted (JUL-2020) 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:MBB1087571.1}.
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DR   EMBL; JACHTE010000002; MBB1087571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7W3YDW2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000552587; 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   FunFam; 3.40.710.10:FF:000021; Penicillin-binding protein 1C; 1.
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:UP000552587};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          70..239
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          317..534
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          711..791
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   795 AA;  86245 MW;  A4FEB61DBA35D14A CRC64;
     MAPMRPRSGA ASGGRARRGG LWCALVVMLL VDAGMLADLA FPLPLPDPRE GGTVVVASNG
     APLRMFADRE GIWRHPVDPG QVSGLYLQAL LAYEDRHFRH HPGINPVALA RAGWQWLREG
     RVVSGGSTLT MQVARILDPP KGSSRTASAK LRQMARALQI EAHLSKDEIL SLYLNRAPFG
     GTIEGVEAAS WAYLGKPASR LSRAEAALLV VLPQAPSRWR PDREPARARQ ARDKVLARMA
     DLGVWTRAEV EDARIEPVVA RDLHAPRHAA LLARRLKAAD PDRRRIESTL DFDLQRTLES
     RVASYFSALP ARTSAALLVI DNASMEARAY VGSVAFADRQ RLGHVDMVRA WRSPGSTLKP
     FLYGLAIDDG LIHSGSLLVD APQSFGDYRP GNFDAAFRGP VTTATALQLS LNVPAVDVLD
     RVGPARFAAR LAHAGIDLRW PRGSRPNLSM ILGGTGARLE DLVGAYAALN REGRAGRVRY
     RPDDTLDDRR LLSPEAAWIV RRMLEDHPRP GSADSFDESG RARVAWKTGT SYGFRDAWAL
     GGTRSHTVGV WVGRPDGTSL PGQYGAITAL PLLFEIIDAL PMHASDARPA PPPAGVARHK
     VCWPLGQLYE ATVPGACRRR IDAWTLADVV PPTLPERDAR LWSAGLARFD VDAVSGERLS
     ANCDADHPRR AAVVARWPAL ATPWLSVAER RAARLPPLAD DCLDDGREGL AELRIDGLHP
     RAILAAAPGA SSGLRLRVRA LGSDARIRWL LDGRLVGESV GSARFEHDFG NPGLHTLTAL
     AETGAWASVE FRVLK
//
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