ID A0A1U9NFS9_9GAMM Unreviewed; 788 AA.
AC A0A1U9NFS9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=B0D95_16270 {ECO:0000313|EMBL:AQT62489.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Cellvibrionales; Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT62489.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT62489.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT62489.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
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}.
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DR EMBL; CP019799; AQT62489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NFS9; -.
DR STRING; 1945512.B0D95_16270; -.
DR KEGG; ceb:B0D95_16270; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000189646; Chromosome.
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:UP000189646};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 49..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..536
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 695..780
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 788 AA; 87939 MW; 117050B7F20E3E18 CRC64;
MVFSSLVGAL VLGVLALHYW PLPQSLTQTP YATMLLARDK SLLGASIATD QQWRFAPVEN
LPDKYKTSLL LFEDQYFYQH PGINPFALLR ALQGNYAAGK VTSGGSTLSM QLARLLRQAD
YQQHDLPLPM RNVPSKAIEA ARALQLEWHF TKDELLIHYA SHAPFGGNIV GLRAAAWRYF
GRAPENLSWS ESALLAVLPN SPALIHPGRQ RDKLLHKRNR LLTRLHQQGH FSALDLQLAL
LEPLPERPAA LPNSASHLLA TLKKQHHSSA LLESTIDATL QRLLNQIAAR HSARLANEGA
HNLALLLIDH STMETLAYVG NQPWNNTARF APDLDLIQRP RSTGSILKPL LYGLMLQSGE
LTPTRLIPDI PSQFGGYSPR NYDRQFRGAV PAQFALAHSL NIPAVYMLRD YGIGRLQKQL
QSMGMSTLFR PADDYGLTLI LGGAEGTLWD LTGIYARLAA SARDGDIPQA PVTLVKTASA
KTLALASIPP VIKQGAAWLT LQALIDVARP GYDNYWRDFS GSQTIAWKTG TSYGLRDAWA
IGSNGRYTLG VWVGNADGEP ATFLSGQSSA APVLFDVFDA LPKINWFAKP QHALKTISVC
DDDGYLAGGQ CTAVDTEVPR TSHFAQVTPY HRRIHLDANE QFRVHSQCEA VSNMQSKNWF
VLPPAQEFYW RQHHSHYKPL PPWRRDCVAN LNQLDDDQPI ELLYPQTQSR IYIPMDLDGK
RSRAVLKAVH RDSAATLYWH LDDAFIGETR IFHEREVALE PGLHQLVIVD QQGYRLQRRF
RVVGKSDQ
//
